1. (2S)-2-Aminopentanedioate
2. (2S)-2-Aminopentanedioic acid
3. (S)-(+)-Glutamate
4. (S)-(+)-Glutamic acid
5. (S)-2-Aminopentanedioate
6. (S)-2-Aminopentanedioic acid
7. (S)-Glutamate
8. (S)-Glutamic acid
9. 1-Aminopropane-1,3-dicarboxylate
10. 1-Aminopropane-1,3-dicarboxylic acid
11. 1-amino-propane-1,3-dicarboxylate
12. 1-amino-propane-1,3-dicarboxylic acid
13. 2-Aminoglutarate
14. 2-Aminoglutaric acid
15. 2-Aminopentanedioate
16. 2-Aminopentanedioic acid
17. Aciglut
18. E
19. Glusate
20. Glutacid
21. Glutamicol
22. Glutamidex
23. Glutaminate
24. Glutaminic acid
25. Glutaminol
26. Glutaton
27. L-(+)-Glutamate
28. L-(+)-Glutamic acid
29. L-Glutamate
30. L-Glutaminate
31. L-Glutaminic acid
32. L-a-Aminoglutarate
33. L-a-Aminoglutaric acid
34. L-glu
35. a-Aminoglutarate
36. a-Aminoglutaric acid
37. a-Glutamate
38. a-Glutamic acid
39. aminoglutarate
40. aminoglutaric acid
41. glt
42. glu
43. glut
44. L-alpha-Aminoglutarate
45. L-alpha-Aminoglutaric acid
46. alpha-Aminoglutarate
47. alpha-Aminoglutaric acid
48. alpha-Glutamate
49. alpha-Glutamic acid

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• Cytoplasm (Predicted from LogP)
• endoplasmic reticulum
• Extracellular
• lysosome
• mitochondria

• Blood
• Cellular Cytoplasm
• Cerebrospinal Fluid
• Saliva
• Urine

• 104300 (Alzheimer's disease)
• 312750 (Rett syndrome)
• 181500 (Schizophrenia)

1. Mross K, Maessen P, van der Vijgh WJ, Gall H, Boven E, Pinedo HM: Pharmacokinetics and metabolism of epidoxorubicin and doxorubicin in humans. J Clin Oncol. 1988 Mar;6(3):517-26. [PubMed ]
2. Noorlander CW, de Graan PN, Nikkels PG, Schrama LH, Visser GH: Distribution of glutamate transporters in the human placenta. Placenta. 2004 Jul;25(6):489-95. [PubMed ]
3. Peng CT, Wu KH, Lan SJ, Tsai JJ, Tsai FJ, Tsai CH: Amino acid concentrations in cerebrospinal fluid in children with acute lymphoblastic leukemia undergoing chemotherapy. Eur J Cancer. 2005 May;41(8):1158-63. Epub 2005 Apr 14. [PubMed ]
4. Grasselli G, Vigano L, Capri G, Locatelli A, Tarenzi E, Spreafico C, Bertuzzi A, Giani A, Materazzo C, Cresta S, Perotti A, Valagussa P, Gianni L: Clinical and pharmacologic study of the epirubicin and paclitaxel combination in women with metastatic breast cancer. J Clin Oncol. 2001 Apr 15;19(8):2222-31. [PubMed ]
5. Cynober LA: Plasma amino acid levels with a note on membrane transport: characteristics, regulation, and metabolic significance. Nutrition. 2002 Sep;18(9):761-6. [PubMed ]
6. Rainesalo S, Keranen T, Palmio J, Peltola J, Oja SS, Saransaari P: Plasma and cerebrospinal fluid amino acids in epileptic patients. Neurochem Res. 2004 Jan;29(1):319-24. [PubMed ]
7. Zupke C, Sinskey AJ, Stephanopoulos G: Intracellular flux analysis applied to the effect of dissolved oxygen on hybridomas. Appl Microbiol Biotechnol. 1995 Dec;44(1-2):27-36. [PubMed ]
8. Molinari F, Raas-Rothschild A, Rio M, Fiermonte G, Encha-Razavi F, Palmieri L, Palmieri F, Ben-Neriah Z, Kadhom N, Vekemans M, Attie-Bitach T, Munnich A, Rustin P, Colleaux L: Impaired mitochondrial glutamate transport in autosomal recessive neonatal myoclonic epilepsy. Am J Hum Genet. 2005 Feb;76(2):334-9. Epub 2004 Dec 8. [PubMed ]
9. Frayn KN, Khan K, Coppack SW, Elia M: Amino acid metabolism in human subcutaneous adipose tissue in vivo. Clin Sci (Lond). 1991 May;80(5):471-4. [PubMed ]
10. Silwood CJ, Lynch E, Claxson AW, Grootveld MC: 1H and (13)C NMR spectroscopic analysis of human saliva. J Dent Res. 2002 Jun;81(6):422-7. [PubMed ]
11. Alfredsson G, Wiesel FA, Tylec A: Relationships between glutamate and monoamine metabolites in cerebrospinal fluid and serum in healthy volunteers. Biol Psychiatry. 1988 Apr 1;23(7):689-97. [PubMed ]
12. Zoia C, Cogliati T, Tagliabue E, Cavaletti G, Sala G, Galimberti G, Rivolta I, Rossi V, Frattola L, Ferrarese C: Glutamate transporters in platelets: EAAT1 decrease in aging and in Alzheimer's disease. Neurobiol Aging. 2004 Feb;25(2):149-57. [PubMed ]
13. Nicholson JK, O'Flynn MP, Sadler PJ, Macleod AF, Juul SM, Sonksen PH: Proton-nuclear-magnetic-resonance studies of serum, plasma and urine from fasting normal and diabetic subjects. Biochem J. 1984 Jan 15;217(2):365-75. [PubMed ]
14. Rizzo V, Anesi A, Montalbetti L, Bellantoni G, Trotti R, Melzi d'Eril GV: Reference values of neuroactive amino acids in the cerebrospinal fluid by high-performance liquid chromatography with electrochemical and fluorescence detection. J Chromatogr A. 1996 Apr 5;729(1-2):181-8. [PubMed ]
15. Agnati LF, Ferre S, Lluis C, Franco R, Fuxe K: Molecular mechanisms and therapeutical implications of intramembrane receptor/receptor interactions among heptahelical receptors with examples from the striatopallidal GABA neurons. Pharmacol Rev. 2003 Sep;55(3):509-50. Epub 2003 Jul 17. [PubMed ]
16. Rutten EP, Engelen MP, Wouters EF, Schols AM, Deutz NE: Metabolic effects of glutamine and glutamate ingestion in healthy subjects and in persons with chronic obstructive pulmonary disease. Am J Clin Nutr. 2006 Jan;83(1):115-23. [PubMed ]
17. Agarwal A, Tripathi LM, Pandey VC: Status of ammonia, glutamate, lactate and pyruvate during Plasmodium yoelii infection and pyrimethamine treatment in mice. J Commun Dis. 1997 Sep;29(3):235-41. [PubMed ]
18. Heuschen UA, Allemeyer EH, Hinz U, Langer K, Heuschen G, Decker-Baumann C, Herfarth C, Stern J: Glutamine distribution in patients with ulcerative colitis and in patients with familial adenomatous polyposis coli before and after restorative proctocolectomy. Int J Colorectal Dis. 2002 Jul;17(4):245-52. Epub 2001 Dec 18. [PubMed ]
19. Olson RC: A proposed role for nerve growth factor in the etiology of multiple sclerosis. Med Hypotheses. 1998 Dec;51(6):493-8. [PubMed ]
20. Nakamura K, Matsumura K, Kobayashi S, Kaneko T: Sympathetic premotor neurons mediating thermoregulatory functions. Neurosci Res. 2005 Jan;51(1):1-8. [PubMed ]
21. Wikipedia

1. Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial precursor
2. Glutathione reductase, mitochondrial precursor
3. Glucosamine--fructose-6-phosphate aminotransferase [isomerizing] 2
4. 4-aminobutyrate aminotransferase, mitochondrial precursor
5. Aspartate aminotransferase, cytoplasmic
6. Aspartate aminotransferase, mitochondrial precursor
7. Branched-chain-amino-acid aminotransferase, cytosolic
8. Alanine--glyoxylate aminotransferase 2, mitochondrial precursor
9. Ornithine aminotransferase, mitochondrial precursor
10. Glutamate--cysteine ligase catalytic subunit
11. N-acetylglutamate synthase, mitochondrial precursor
12. Branched-chain-amino-acid aminotransferase, mitochondrial precursor
13. Bifunctional aminoacyl-tRNA synthetase [Includes: Glutamyl-tRNA synthetase
14. Asparagine synthetase [glutamine-hydrolyzing]
15. Glutamate dehydrogenase 2, mitochondrial precursor
16. Glutamine synthetase
17. CTP synthase 1
18. Glutaminase kidney isoform, mitochondrial precursor
19. Formimidoyltransferase-cyclodeaminase
20. Glutamate dehydrogenase 1, mitochondrial precursor
21. Glutamate decarboxylase 2
22. Glutamate decarboxylase 1
23. Gamma-glutamyltranspeptidase 1 precursor
24. Glutathione synthetase
25. Folylpolyglutamate synthase, mitochondrial precursor
26. Delta 1-pyrroline-5-carboxylate synthetase
27. 5-oxoprolinase
28. Glutamate [NMDA] receptor subunit zeta-1 precursor
29. Glutamate [NMDA] receptor subunit 3B precursor
30. Glutamate [NMDA] receptor subunit epsilon-2 precursor
31. Vitamin K-dependent gamma-carboxylase
32. Glutamate receptor, ionotropic kainate 2 precursor
33. Glutamate carboxypeptidase 2
34. Metabotropic glutamate receptor 1 precursor
35. Arginine decarboxylase
36. L-glutaminase
37. Hypothetical protein GAD1
38. Hypothetical protein AADAT
39. Excitatory amino acid transporter 3
40. Mitochondrial glutamate carrier 2
41. Glutamine-dependent NAD(+) synthetase
42. CAD protein [Includes: Glutamine-dependent carbamoyl-phosphate synthase
43. Alanine aminotransferase 2
44. Alanine aminotransferase
45. Gamma-glutamyltransferase 6 homolog
46. cDNA FLJ78123, highly similar to Homo sapiens phosphoribosyl pyrophosphate amidotransferase
47. cDNA FLJ75406, highly similar to Homo sapiens guanine monphosphate synthetase
48. Glutamine synthetase
49. Probable glutamyl-tRNA synthetase, mitochondrial precursor
50. Phosphoserine aminotransferase 1
51. Aminoadipate-semialdehyde synthase
52. cDNA, FLJ96771, Homo sapiens ornithine decarboxylase-like protein (ODC-p), mRNA (Arginine decarboxylase, isoform CRA_d)
53. cDNA, FLJ95223, Homo sapiens N-acetylglutamate synthase (NAGS), mRNA
54. GGTL3 protein (Fragment)
55. Gamma-glutamyltransferase-like activity 1
56. Putative uncharacterized protein GFPT1
57. cDNA FLJ75059, highly similar to Homo sapiens phosphoribosylformylglycinamidine synthase (FGAR amidotransferase) (PFAS), mRNA
58. cDNA, FLJ95372, highly similar to Homo sapiens branched chain aminotransferase 2, mitochondrial(BCAT2), mRNA (Branched chain aminotransferase 2, mitochondrial)
59. cDNA FLJ43342 fis, clone NT2RI3007978, highly similar to CTP synthase 2 (EC 6.3.4.2)
60. cDNA, FLJ93078, Homo sapiens glutamic-oxaloacetic transaminase 1, soluble(aspartate aminotransferase 1) (GOT1), mRNA (Glutamic-oxaloacetic transaminase 1, soluble (Aspartate aminotransferase 1), isoform CRA_b)
61. cDNA, FLJ93913, Homo sapiens tyrosine aminotransferase (TAT), nuclear gene encodingmitochondrial protein, mRNA (Tyrosine aminotransferase, isoform CRA_a)
62. Aspartyl aminopeptidase
63. Metabotropic glutamate receptor 8
64. Metabotropic glutamate receptor 4
65. Metabotropic glutamate receptor 7

1. P5C dehydrogenase
2. Aldehyde dehydrogenase 4A1

MLLPAPALRRALLSRPWTGAGLRWKHTSSLKVANEPVLAFTQGSPERDALQKALKDLKGR
MEAIPCVVGDEEVWTSDVQYQVSPFNHGHKVAKFCYADKSLLNKAIEAALAARKEWDLKP
IADRAQIFLKAADMLSGPRRAEILAKTMVGQGKTVIQAEIDAAAELIDFFRFNAKYAVEL
EGQQPISVPPSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALMGNVVLWKPSDTAML
ASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQ
NLDRFHTFPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSL
WPQIKGRLLEEHSRIKVGDPAEDFGTFFSAVIDAKSFARIKKWLEHARSSPSLTILAGGK
CDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDKYKETLQLVDSTTSYGLTG
AVFSQDKDVVQEATKVLRNAAGNFYINDKSTGSIVGQQPFGGARASGTNDKPGGPHYILR
WTSPQVIKETHKPLGDWSYAYMQ

• Arginine and Proline Metabolism (map00330 )
• Glutamate Metabolism (map00251 )

• 1-pyrroline-5-carboxylate + NAD+ + H2O = L-glutamate + NADH + H+

• Aldedh (PF00171 )

• 1-19

ATGCTGCTGCCGGCGCCCGCGCTCCGCCGCGCCCTGCTGTCCCGCCCCTGGACCGGGGCC
GGCCTGCGGTGGAAGCACACCTCCTCCCTGAAGGTGGCCAACGAGCCCGTCTTAGCCTTC
ACGCAGGGCAGCCCTGAGCGAGATGCCCTGCAAAAGGCCTTGAAGGACCTGAAGGGCCGG
ATGGAAGCCATCCCATGCGTGATGGGGGATGAGGAGGTGTGGACGTCGGACGTGCAGTAC
CAAGTGTCGCCTTTTAACCATGGACATAAGGTGGCCAAGTTCTGTTATGCAGACAAGAGC
CTGCTCAACAAAGCCATTGAGGCTGCCCTGGCTGCCCGGAAAGAGTGGGACCTGAAGCCT
ATTGCAGACCGGGCCCAGATCTTCCTGAAGGCGGCAGACATGCTGAGTGGGCCGCGCAGG
GCTGAGATCCTCGCCAAGACCATGGTGGGACAGGGTAAGACCGTGATCCAAGCGGAGATT
GACGCTGCAGCGGAACTCATCGACTTCTTCCGGTTCAATGCCAAGTATGCGGTGGAGCTG
GAGGGGCAGCAGCCCATCAGCGTGCCCCCGAGCACCAACAGCACGGTGTACCGGGGTCTG
GAGGGCTTCGTGGCGGCCATCTCGCCCTTTAACTTCACTGCAATCGGCGGCAACCTGGCG
GGGGCACCGGCCCTGATGGGCAACGTGGTCCTATGGAAGCCCAGTGACACTGCCATGCTG
GCCAGCTATGCTGTCTACCGCATCCTTCGGGAGGCTGGCCTGCCCCCCAACATCATCCAG
TTTGTGCCAGCTGATGGGCCCCTATTTGGGGACACTGTCACCAGCTCAGAGCACCTCTGT
GGCATCAACTTCACAGGCAGTGTGCCCACCTTCAAACACCTGTGGAAGCAGGTGGCCCAG
AACCTGGACCGGTTCCACACCTTCCCACGCCTGGCTGGAGAGTGCGGCGGAAAGAACTTC
CACTTCGTGCACCGCTCGGCCGACGTGGAGAGCGTGGTGAGCGGGACCCTCCGCTCAGCC
TTCGAGTACGGTGGCCAGAAGTGTTCCGCCTGCTCGCGTCTCTACGTGCCGCACTCGCTG
TGGCCGCAGATCAAAGGGCGGCTGCTGGAGGAGCACAGTCGGATCAAAGTGGGCGACCCT
GCAGAGGATTTTGGGACCTTCTTCTCTGCAGTGATTGATGCCAAGTCCTTTGCCCGTATC
AAGAAGTGGCTGGAGCACGCGCGCTCCTCGCCCAGCCTCACCATCCTGGCTGGGGGCAAG
TGTGATGACTCCGTGGGCTACTTTGTGGAGCCCTGCATCGTGGAGAGCAAGGACCCTCAG
GAGCCCATCATGAAGGAGGAGATCTTCGGGCCTGTACTGTCTGTGTACGTCTACCCGGAC
GACAAGTACAAGGAGACGCTGCAGCTGGTTGACAGCACCACCAGCTATGGCCTCACGGGG
GCAGTGTTCTCCCAGGATAAGGACGTCGTGCAGGAGGCCACAAAGGTGCTGAGGAATGCT
GCCGGCAACTTCTACATCAACGACAAGTCCACTGGCTCGATAGTGGGCCAGCAGCCCTTT
GGGGGGGCCCGAGCCTCTGGAACCAATGACAAGCCAGGGGGCCCACACTACATCCTGCGC
TGGACGTCGCCGCAGGTCATCAAGGAGACACATAAGCCCCTGGGGGACTGGAGCTACGCG
TACATGCAGTGA

1. Hu CA, Lin WW, Valle D: Cloning, characterization, and expression of cDNAs encoding human delta 1-pyrroline-5-carboxylate dehydrogenase. J Biol Chem. 1996 Apr 19;271(16):9795-800. [PubMed ]
2. Hempel J, Eckey R, Berie D, Romovacek H, Agarwal DP, Goedde HW: Human liver glutamic gamma-semialdehyde dehydrogenase: structural relationship to the yeast enzyme. Comp Biochem Physiol B. 1992 Aug;102(4):791-93. [PubMed ]
3. Hochstrasser DF, Frutiger S, Paquet N, Bairoch A, Ravier F, Pasquali C, Sanchez JC, Tissot JD, Bjellqvist B, Vargas R, et al.: Human liver protein map: a reference database established by microsequencing and gel comparison. Electrophoresis. 1992 Dec;13(12):992-1001. [PubMed ]
4. Geraghty MT, Vaughn D, Nicholson AJ, Lin WW, Jimenez-Sanchez G, Obie C, Flynn MP, Valle D, Hu CA: Mutations in the Delta1-pyrroline 5-carboxylate dehydrogenase gene cause type II hyperprolinemia. Hum Mol Genet. 1998 Sep;7(9):1411-5. [PubMed ]

1. GR
2. GRase

MALLPRALSAGAGPSWRRAARAFRGFLLLLPEPAALTRALSRAMACRQEPQPQGPPPAAG
AVASYDYLVIGGGSGGLASARRAAELGARAAVVESHKLGGTCVNVGCVPKKVMWNTAVHS
EFMHDHADYGFPSCEGKFNWRVIKEKRDAYVSRLNAIYQNNLTKSHIEIIRGHAAFTSDP
KPTIEVSGKKYTAPHILIATGGMPSTPHESQIPGASLGITSDGFFQLEELPGRSVIVGAG
YIAVEMAGILSALGSKTSLMIRHDKVLRSFDSMISTNCTEELENAGVEVLKFSQVKEVKK
TLSGLEVSMVTAVPGRLPVMTMIPDVDCLLWAIGRVPNTKDLSLNKLGIQTDDKGHIIVD
EFQNTNVKGIYAVGDVCGKALLTPVAIAAGRKLAHRLFEYKEDSKLDYNNIPTVVFSHPP
IGTVGLTEDEAIHKYGIENVKTYSTSFTPMYHAVTKRKTKCVMKMVCANKEEKVVGIHMQ
GLGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSEELVTLR

• Glutamate Metabolism (map00251 )
• Glutathione Metabolism (map00480 )

• 2 glutathione + NADP+ = glutathione disulfide + NADPH + H+

• Pyr_redox (PF00070 )
• Pyr_redox_2 (PF07992 )
• Pyr_redox_dim (PF02852 )

• 1-37

ATGGCCTGCAGGCAGGAGCCGCAGCCGCAGGGCCCGCCGCCCGCTGCTGGCGCCGTGGCC
TCCTATGACTACCTGGTGATCGGGGGCGGCTCGGGCGGGCTGGCCAGCGCGCGCAGGGCG
GCCGAGCTGGGTGCCAGGGCCGCCGTGGTGGAGAGCCACAAGCTGGGTGGCACTTGCGTG
AATGTTGGATGTGTACCCAAAAAGGTAATGTGGAACACAGCTGTCCACTCTGAATTCATG
CATGATCATGCTGATTATGGCTTTCCAAGTTGTGAGGGTAAATTCAATTGGCGTGTTATT
AAGGAAAAGCGGGATGCCTATGTGAGCCGCCTGAATGCCATCTATCAAAACAATCTCACC
AAGTCCCATATAGAAATCATCCGTGGCCATGCAGCCTTCACGAGTGATCCCAAGCCCACA
ATAGAGGTCAGTGGGAAAAAGTACACCGCCCCACACATCCTGATCGCCACAGGTGGTATG
CCCTCCACCCCTCATGAGAGCCAGATCCCCGGTGCCAGCTTAGGAATAACCAGCGATGGA
TTTTTTCAGCTGGAAGAATTGCCCGGCCGCAGCGTCATTGTTGGTGCAGGTTACATTGCT
GTGGAGATGGCAGGGATCCTGTCAGCCCTGGGTTCTAAGACATCACTGATGATACGGCAT
GATAAGGTACTTAGAAGTTTTGATTCAATGATCAGCACCAACTGCACGGAGGAGCTGGAG
AACGCTGGCGTGGAGGTGCTGAAGTTCTCCCAGGTCAAGGAGGTTAAAAAGACTTTGTCG
GGCTTGGAAGTCAGCATGGTTACTGCAGTTCCCGGTAGGCTACCAGTCATGACCATGATT
CCAGATGTTGACTGCCTGCTCTGGGCCATTGGGCGGGTCCCGAATACCAAGGACCTGAGT
TTAAACAAACTGGGGATTCAAACCGATGACAAGGGTCATATCATCGTAGACGAATTCCAG
AATACCAACGTCAAAGGCATCTATGCAGTTGGGGATGTATGTGGAAAAGCTCTTCTTACT
CCAGTTGCAATAGCTGCTGGCCGAAAACTTGCCCATCGACTTTTTGAATATAAGGAAGAT
TCCAAATTAGATTATAACAACATCCCAACTGTGGTCTTCAGCCACCCCCCTATTGGGACA
GTGGGACTCACGGAAGATGAAGCCATTCATAAATATGGAATAGAAAATGTGAAGACCTAT
TCAACGAGCTTTACCCCGATGTATCACGCAGTTACCAAAAGGAAAACAAAATGTGTGATG
AAAATGGTCTGTGCTAACAAGGAAGAAAAGGTGGTTGGGATCCATATGCAGGGACTTGGG
TGTGATGAAATGCTGCAGGGTTTTGCTGTTGCAGTGAAGATGGGAGCAACGAAGGCAGAC
TTTGACAACACAGTCGCCATTCACCCTACCTCTTCAGAAGAGCTGGTCACACTTCGTTGA

1. Tutic M, Lu XA, Schirmer RH, Werner D: Cloning and sequencing of mammalian glutathione reductase cDNA. Eur J Biochem. 1990 Mar 30;188(3):523-8. [PubMed ]
2. Kelner MJ, Montoya MA: Structural organization of the human glutathione reductase gene: determination of correct cDNA sequence and identification of a mitochondrial leader sequence. Biochem Biophys Res Commun. 2000 Mar 16;269(2):366-8. [PubMed ]
3. Krauth-Siegel RL, Blatterspiel R, Saleh M, Schiltz E, Schirmer RH, Untucht-Grau R: Glutathione reductase from human erythrocytes. The sequences of the NADPH domain and of the interface domain. Eur J Biochem. 1982 Jan;121(2):259-67. [PubMed ]
4. Krohne-Ehrich G, Schirmer RH, Untucht-Grau R: Glutathione reductase from human erythrocytes. Isolation of the enzyme and sequence analysis of the redox-active peptide. Eur J Biochem. 1977 Oct 17;80(1):65-71. [PubMed ]
5. Thieme R, Pai EF, Schirmer RH, Schulz GE: Three-dimensional structure of glutathione reductase at 2 A resolution. J Mol Biol. 1981 Nov 15;152(4):763-82. [PubMed ]
6. Karplus PA, Schulz GE: Refined structure of glutathione reductase at 1.54 A resolution. J Mol Biol. 1987 Jun 5;195(3):701-29. [PubMed ]
7. Savvides SN, Karplus PA: Kinetics and crystallographic analysis of human glutathione reductase in complex with a xanthene inhibitor. J Biol Chem. 1996 Apr 5;271(14):8101-7. [PubMed ]
8. Stoll VS, Simpson SJ, Krauth-Siegel RL, Walsh CT, Pai EF: Glutathione reductase turned into trypanothione reductase: structural analysis of an engineered change in substrate specificity. Biochemistry. 1997 May 27;36(21):6437-47. [PubMed ]
9. Becker K, Savvides SN, Keese M, Schirmer RH, Karplus PA: Enzyme inactivation through sulfhydryl oxidation by physiologic NO-carriers. Nat Struct Biol. 1998 Apr;5(4):267-71. [PubMed ]

1. Hexosephosphate aminotransferase 2
2. D-fructose-6- phosphate amidotransferase 2
3. GFAT 2
4. GFAT2

MCGIFAYMNYRVPRTRKEIFETLIKGLQRLEYRGYDSAGVAIDGNNHEVKERHIQLVKKR
GKVKALDEELYKQDSMDLKVEFETHFGIAHTRWATHGVPSAVNSHPQRSDKGNEFVVIHN
GIITNYKDLRKFLESKGYEFESETDTETIAKLIKYVFDNRETEDITFSTLVERVIQQLEG
AFALVFKSVHYPGEAVATRRGSPLLIGVRSKYKLSTEQIPILYRTCTLENVKNICKTRMK
RLDSSACLHAVGDKAVEFFFASDASAIIEHTNRVIFLEDDDIAAVADGKLSIHRVKRSAS
DDPSRAIQTLQMELQQIMKGNFSAFMQKEIFEQPESVFNTMRGRVNFETNTVLLGGLKDH
LKEIRRCRRLIVIGCGTSYHAAVATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFF
ISQSGETADTLLALRYCKDRGALTVGVTNTVGSSISRETDCGVHINAGPEIGVASTKAYT
SQFISLVMFGLMMSEDRISLQNRRQEIIRGLRSLPELIKEVLSLEEKIHDLALELYTQRS
LLVMGRGYNYATCLEGALKIKEITYMHSEGILAGELKHGPLALIDKQMPVIMVIMKDPCF
AKCQNALQQVTARQGRPIILCSKDDTESSKFAYKTIELPHTVDCLQGILSVIPLQLLSFH
LAVLRGYDVDFPRNLAKSVTVE

• Aminosugars metabolism (map00530 )
• Glutamate Metabolism (map00251 )

• L-glutamine + D-fructose 6-phosphate = L-glutamate + D-glucosamine 6-phosphate

• GATase_2 (PF00310 )
• SIS (PF01380 )

• None

• None

ATGTGCGGAATCTTTGCCTACATGAACTACAGAGTCCCCCGGACGAGGAAGGAGATCTTC
GAAACCCTCATCAAGGGCCTGCAGCGGCTGGAGTACAGAGGCTACGACTCGGCAGGTGTG
GCGATCGATGGGAATAATCACGAAGTCAAAGAAAGACACATTCAGCTGGTCAAGAAAAGG
GGGAAAGTCAAGGCTCTCGATGAAGAACTTTACAAACAAGACAGCATGGACTTAAAAGTG
GAGTTTGAGACACACTTCGGCATTGCCCACACGCGCTGGGCCACCCACGGGGTCCCCAGT
GCTGTCAACAGCCACCCTCAGCGCTCAGACAAAGGCAACGAATTTGTTGTCATCCACAAT
GGGATCATCACAAATTACAAAGATCTGAGGAAATTTCTGGAAAGCAAAGGCTACGAGTTT
GAGTCAGAAACAGATACAGAGACCATCGCCAAGCTGATTAAATATGTGTTCGACAACAGA
GAAACTGAGGACATTACGTTTTCAACGTTGGTCGAGAGAGTCATTCAGCAGTTGGAAGGT
GCATTCGCGCTGGTTTTCAAGAGTGTCCACTACCCAGGAGAAGCCGTTGCCACACGGAGA
GGCAGCCCCCTGCTCATCGGAGTCCGGAGCAAATACAAGCTCTCCACAGAACAGATCCCT
ATCTTATACAGGACGTGCACTCTGGAGAATGTGAAGAATATCTGTAAGACACGGATGAAG
AGGCTGGACAGCTCCGCCTGCCTGCATGCTGTGGGCGACAAGGCCGTGGAATTCTTCTTT
GCTTCTGATGCAAGCGCTATCATAGAGCACACCAACCGGGTCATCTTCCTGGAGGACGAT
GACATCGCCGCAGTGGCTGATGGGAAACTCTCCATTCACCGGGTCAAGCGCTCGGCCAGT
GATGACCCATCTCGAGCCATCCAGACCTTGCAGATGGAACTGCAGCAAATCATGAAAGGT
AACTTCAGTGCGTTTATGCAGAAGGAGATCTTCGAACAGCCAGAATCAGTTTTCAATACT
ATGAGAGGTCGGGTGAATTTTGAAACCAACACAGTGCTCCTGGGTGGCTTGAAGGACCAC
TTGAAGGAGATTCGACGATGCCGACGGCTCATCGTGATTGGCTGTGGAACCAGCTACCAC
GCTGCCGTGGCTACGCGGCAAGTTTTGGAGGAACTGACTGAGCTTCCTGTGATGGTTGAA
CTTGCTAGTGATTTTCTGGACAGGAACACACCTGTGTTCAGGGATGACGTTTGCTTTTTC
ATCAGCCAGTCAGGCGAGACCGCGGACACCCTCCTGGCGCTGCGCTACTGTAAGGACCGC
GGCGCTCTCACCGTGGGCGTCACCAACACCGTGGGCAGCTCCATCTCTCGCGAGACCGAC
TGCGGCGTCCACATCAACGCAGGGCCGGAGATCGGCGTGGCCAGCACCAAGGCTTATACC
AGTCAGTTCATCTCTCTGGTGATGTTTGGTTTGATGATGTCTGAAGACCGAATTTCACTA
CAAAACAGGAGGCAAGAGATCATCCGTGGCTTGAGATCTTTACCTGAGCTGATCAAGGAA
GTGCTGTCTCTGGAGGAGAAGATCCACGACTTGGCCCTGGAGCTCTACACGCAGAGATCG
CTGCTGGTGATGGGGCGGGGCTACAACTATGCCACCTGCCTGGAAGGAGCCCTGAAAATT
AAAGAGATAACCTACATGCACTCAGAAGGCATCCTGGCTGGGGAGCTGAAGCACGGGCCC
CTGGCACTGATTGACAAGCAGATGCCCGTCATCATGGTCATTATGAAGGATCCTTGCTTC
GCCAAATGCCAGAACGCCCTGCAGCAAGTCACGGCCCGCCAGGGTCGCCCCATTATACTG
TGCTCCAAGGACGATACTGAAAGTTCCAAGTTTGCGTATAAGACAATTGAGCTGCCCCAC
ACTGTGGACTGCCTCCAGGGCATCCTGAGCGTGATTCCGCTGCAGCTGCTGTCCTTCCAC
CTGGCTGTTCTCCGAGGATATGACGTTGACTTCCCCAGAAATCTGGCCAAGTCTGTAACT
GTGGAATGA

1. Oki T, Yamazaki K, Kuromitsu J, Okada M, Tanaka I: cDNA cloning and mapping of a novel subtype of glutamine:fructose-6-phosphate amidotransferase (GFAT2) in human and mouse. Genomics. 1999 Apr 15;57(2):227-34. [PubMed ]

1. (S-3-amino-2-methylpropionate transaminase
2. Gamma-amino-N-butyrate transaminase
3. GABA transaminase
4. GABA aminotransferase
5. GABA-AT
6. GABA-T
7. L-AIBAT

MASMLLAQRLACSFQHSYRLLVPGSRHISQAAAKVDVEFDYDGPLMKTEVPGPRSQELMK
QLNIIQNAEAVHFFCNYEESRGNYLVDVDGNRMLDLYSQISSVPIGYSHPALLKLIQQPQ
NASMFVNRPALGILPPENFVEKLRQSLLSVAPKGMSQLITMACGSCSNENALKTIFMWYR
SKERGQRGFSQEELETCMINQAPGCPDYSILSFMGAFHGRTMGCLATTHSKAIHKIDIPS
FDWPIAPFPRLKYPLEEFVKENQQEEARCLEEVEDLIVKYRKKKKTVAGIIVEPIQSEGG
DNHASDDFFRKLRDIARKHGCAFLVDEVQTGGGCTGKFWAHEHWGLDDPADVMTFSKKMM
TGGFFHKEEFRPNAPYRIFNTWLGDPSKNLLLAEVINIIKREDLLNNAAHAGKALLTGLL
DLQARYPQFISRVRGRGTFCSFDTPDDSIRNKLILIARNKGVVLGGCGDKSIRFRPTLVF
RDHHAHLFLNIFSDILADFK

• Valine, Leucine and Isoleucine Degradation (map00280 )

• (S)-3-amino-2-methylpropanoate + 2-oxoglutarate = 2-methyl-3-oxopropanoate + L-glutamate

• Aminotran_3 (PF00202 )

• None

• None

ATGGCCTCCATGTTGCTCGCCCAGCGGCTGGCCTGCAGCTTCCAGCACACGTACCGCCTG
CTGGTGCCTGGATCCAGACACATTAGTCAAGCTGCAGCCAAAGTCGACGTTGAATTTGAT
TATGATGGGCCTCTGATGAAGACGGAAGTCCCAGGGCCTAGATCTCAGGAGTTAATGAAA
CAGCTGAATATAATTCAGAATGCAGAGGCTGTGCATTTTTTCTGCAATTACGAAGAGAGC
CGAGGCAATTACCTGGTTGATGTGGACGGCAACCGAATGCTGGATCTTTATTCCCAGATC
TCCTCTGTTCCCATAGGTTACAGCGACCCGGCCCTCGTGAAACTCATCCAACAGCCACAA
AATGCGAGCATGTTTGTCAACAGACCCGCCCTCGAAATCCTGCCTCCGGAGAACTTTGTG
GAGAAGCTCCGGCAGTCCTTGCTCTCGGTGGCTCCCAAAGGGATGTCCCAGCTCATCACC
ATGGCCTGCGGCTCCTGCTCCAATGAAAACGCCTTAAAGACCATCTTCATGTGGTACCGG
AGCAAGGAAAGAGGGCAGAGGGGATTCTCCAAAGAGGAGCTGGAGACGTGCATGATTAAC
CAGGCCCCCTGGTGCCCCGACTACAGCATCCTCTCCTTCATGGGTTCCTTCCATGGGAGG
ACCATGGGTTGCTTAGCGACCACGCACTCTAAAGCCATTCACAAGATCGATATCCCTTCC
TTTGACTGGCCCATCGCACCGTTCCCACGGCTGAAATACCCTCTGGAAGAGTTTGTGAAA
GAGAACCAACAGGAAGAGGCCGGCTGTCTGGAAGAGGTTGAGGATCTGATTGTGAAATAT
CGAAAAAAGAAGAAGACGGTGGCCGGGATCATCGTGGAGCCCATCCAGTCCGAGGGTGGA
GACAACCATGCATCCGATGACTTCTTTCGGAAGCTGAGAGACATCGCCAGGAAGCACTGC
TGCGCCTTCTTGGTGGACGAGGTCCAGACCGGAGGAGGCTGCACGGGCAAGTTCTGGGCC
CATGAGCACTGGGGCCTGGATGACCCAGCAGACGTGATGACCTTCAGCAAGAAGATGATG
ACTGGGGGCTTCTTCCTCAAGGAGGAGTTCAGGCCTAATGCTCCCTACCGGATCTTCAAC
ACGTGGCTGGGGGACCCGTCCAAGAACCTGTTGCTGGCTGAGGTCATCAACATCATCAAG
CGGGAGGACCTGCTAAATAATGCAGCCCATGCCGGGAAGGCCCTGCTCACAGGACTGCTG
GACCTCCAGGCCCGGTACCCCCAGTTCATCAGCAGGGTGAGAGGACGAGGCACCTTTTGC
TCCTTCGATACTCCCGATGATTCCATACGGAATAAGCTCATTTTAATTGCCAGAAACAAA
GGTGTGGTGTTGGGTGGCTGTGGTGACAAATCCATTCGTTTCCGTCCCACGCTGGTGTTC
AGGGATCACCACGCTCACCTGTTCCTCAATATTTTCAGTGACATCTTAGCAGACTTCAAG
TAA

1. Osei YD, Churchich JE: Screening and sequence determination of a cDNA encoding the human brain 4-aminobutyrate aminotransferase. Gene. 1995 Apr 3;155(2):185-7. [PubMed ]
2. De Biase D, Barra D, Simmaco M, John RA, Bossa F: Primary structure and tissue distribution of human 4-aminobutyrate aminotransferase. Eur J Biochem. 1995 Jan 15;227(1-2):476-80. [PubMed ]
3. Medina-Kauwe LK, Tobin AJ, De Meirleir L, Jaeken J, Jakobs C, Nyhan WL, Gibson KM: 4-Aminobutyrate aminotransferase (GABA-transaminase) deficiency. J Inherit Metab Dis. 1999 Jun;22(4):414-27. [PubMed ]

1. Transaminase A
2. Glutamate oxaloacetate transaminase 1

MAPPSVFAEVPQAQPVLVFKLTADFREDPDPRKVNLGVGAYRTDDCHPWVLPVVKKVEQK
IANDNSLNHEYLPILGLAEFRSCASRLALGDDSPALKEKRVGGVQSLGGTGALRIGADFL
ARWYNGTNNKNTPVYVSSPTWENHNAVFSAAGFKDIRSYRYWDAEKRGLDLQGFLNDLEN
APEFSIVVLHACAHNPTGIDPTPEQWKQIASVMKHRFLFPFFDSAYQGFASGNLERDAWA
IRYFVSEGFEFFCAQSFSKNFGLYNERVGNLTVVGKEPESILQVLSQMEKIVRITWSNPP
AQGARIVASTLSNPELFEEWTGNVKTMADRILTMRSELRARLEALKTPGTWNHITDQIGM
FSFTGLNPKQVEYLVNEKHIYLLPSGRINVSGLTTKNLDYVATSIHEAVTKIQ

• Arginine and Proline Metabolism (map00330 )
• Carbon fixation (map00710 )
• Cysteine Metabolism (map00272 )
• Glutamate Metabolism (map00251 )
• Phenylalanine Metabolism (map00360 )
• Phenylalanine and Tyrosine Metabolism (map00400 )
• Tyrosine Metabolism (map00350 )
• Novobiocin biosynthesis (map00401 )

• L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate

• Aminotran_1_2 (PF00155 )

• None

• None

ATGGCACCTCCGTCAGTCTTTGCCGAGGTTCCGCAGGCCCAGCCTGTCCTGGTCTTCAAG
CTCACTGCCGACTTCAGGGAGGATCCGGACCCCCGCAAGGTCAACCTGGGAGTGGGAGCA
TATCGCACGGATGACTGCCATCCCTGGGTTTTGCCAGTAGTGAAGAAAGTGGAGCAGAAG
ATTGCTAATGACAATAGCCTAAATCACGAGTATCTGCCAATCCTGGGCCTGGCTGAGTTC
CGGAGCTGTGCTTCTCGTCTTGCCCTTGGGGATGACAGCCCAGCACTCAAGGAGAAGCGG
GTAGGAGGTGTGCAATCTTTGGGGGGAACAGGTGCACTTCGAATTGGAGCTGATTTCTTA
GCGCGTTGGTACAATGGAACAAACAACAAGAACACACCTGTCTATGTGTCCTCACCAACC
TGGGAGAATCACAATGCTGTGTTTTCCGCTGCTGGTTTTAAAGACATTCGGTCCTATCGC
TACTGGGATGCAGAGAAGAGAGGATTGGACCTCCAGGGCTTCCTGAATGATCTGGAGAAT
GCTCCTGAGTTCTCCATTGTTGTCCTCCACGCCTGTGCACACAACCCAACTGGGATTGAC
CCAACTCCGGAGCAGTGGAAGCAGATTGCTTCTGTCATGAAGCACCGGTTTCTGTTCCCC
TTCTTTGACTCAGCCTATCAGGGCTTCGCATCTGGAAACCTGGAGAGAGATGCCTGGGCC
ATTCGCTATTTTGTGTCTGAAGGCTTCGAGTTCTTCTGTGCCCAGTCCTTCTCCAAGAAC
TTCGGGCTCTACAATGAGAGAGTCGGGAATCTGACTGTGGTTGGAAAAGAACCTGAGAGC
ATCCTGCAAGTCCTTTCCCAGATGGAGAAGATCGTGCGGATTACTTGGTCCAATCCCCCC
GCCCAGGGAGCACGAATTGTGGCCAGCACCCTCTCTAACCCTGAGCTCTTTGAGGAATGG
ACAGGTAATGTGAAGACAATGGCTGACCGGATTCTGACCATGAGATCTGAACTCAGGGCA
CGACTAGAAGCCCTCAAAACCCCTGGGACCTGGAACCACATCACTGATCAAATTGGCATG
TTCAGCTTCACTGGGTTGAACCCCAAGCAGGTTGAGTATCTGGTCAATGAAAAGCACATC
TACCTGCTGCCAAGTGGTCGAATCAACGTGAGTGGCTTAACCACCAAAAATCTAGATTAC
GTGGCCACCTCCATCCATGAAGCAGTCACCAAAATCCAGTGA

1. Bousquet-Lemercier B, Pol S, Pave-Preux M, Hanoune J, Barouki R: Properties of human liver cytosolic aspartate aminotransferase mRNAs generated by alternative polyadenylation site selection. Biochemistry. 1990 Jun 5;29(22):5293-9. [PubMed ]
2. Doyle JM, Schinina ME, Bossa F, Doonan S: The amino acid sequence of cytosolic aspartate aminotransferase from human liver. Biochem J. 1990 Sep 15;270(3):651-7. [PubMed ]

1. Transaminase A
2. Glutamate oxaloacetate transaminase 2

MALLHSGRVLPGIAAAFHPGLAAAASARASSWWTHVEMGPPDPILGVTEAFKRDTNSKKM
NLGVGAYRDDNGKPYVLPSVRKAEAQIAAKNLDKEYLPIGGLAEFCKASAELALGENSEV
LKSGRFVTVQTISGTGALRIGASFLQRFFKFSRDVFLPKPTWGNHTPIFRDAGMQLQGYR
YYDPKTCGFDFTGAVEDISKIPEQSVLLLHACAHNPTGVDPRPEQWKEIATVVKKRNLFA
FFDMAYQGFASGDGDKDAWAVRHFIEQGINVCLCQSYAKNMGLYGERVGAFTMVCKDADE
AKRVESQLKILIRPMYSNPPLNGARIAAAILNTPDLRKQWLQEVKGMADRIIGMRTQLVS
NLKKEGSTHNWQHITDQIGMFCFTGLKPEQVERLIKEFSIYMTKDGRISVAGVTSSNVGY
LAHAIHQVTK

• Arginine and Proline Metabolism (map00330 )
• Carbon fixation (map00710 )
• Cysteine Metabolism (map00272 )
• Glutamate Metabolism (map00251 )
• Phenylalanine Metabolism (map00360 )
• Phenylalanine and Tyrosine Metabolism (map00400 )
• Tyrosine Metabolism (map00350 )
• Novobiocin biosynthesis (map00401 )

• L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate

• Aminotran_1_2 (PF00155 )

• 1-24

ATGGCCCTGCTGCACTCCGGCCGCGTCCTCCCCGGGATCGCCGCCGCCTTCCACCCGGGC
CTCGCCGCCGCGGCCTCTGCCAGAGCCAGCTCCTGGTGGACCCATGTGGAAATGGGACCT
CCAGATCCCATTCTGGGAGTCACTGAAGCCTTTAAGAGGGACACCAATAGCAAAAAGATG
AATCTGGGAGTTGGTGCCTACCGGGATGATAATGGAAAGCCTTACGTTCTGCCTAGCGTC
CGCAAGGCAGAGGCCCAGATTGCCGCAAAAAATTTGGACAAGGAATACCTGCCCATTGGG
GGACTGGCTGAATTTTGCAAGGCATCTGCAGAACTAGCCCTGGGTGAGAACAGCGAAGTC
TTGAAGAGTGGCCGGTTTGTCACTGTGCAGACCATTTCTGGAACTGGAGCCTTAAGGATC
GGAGCCAGTTTTCTGCAAAGATTTTTTAAGTTCAGCCGAGATGTCTTTCTGCCCAAACCA
ACCTGGGGAAACCACACACCCATCTTCAGGGATGCTGGCATGCAGCTACAAGGTTATCGG
TATTATGACCCCAAGACTTGCGGTTTTGACTTCACAGGCGCTGTGGAGGATATTTCAAAA
ATACCAGAGCAGAGTGTTCTTCTTCTGCATGCCTGCGCCCACAATCCCACGGGAGTGGAC
CCGCGTCCGGAACAGTGGAAGGAAATAGCAACAGTGGTGAAGAAAAGGAATCTCTTTGCG
TTCTTTGACATGGCCTACCAAGGCTTTGCCAGTGGTGATGGTGATAAGGATGCCTGGGCT
GTGCGCCACTTCATCGAACAGGGCATTAATGTTTGCCTCTGCCAATCATATGCCAAGAAC
ATGGGCTTATATGGTGAGCGTGTAGGAGCCTTCACTATGGTCTGCAAAGATGCGGATGAA
GCCAAAAGGGTAGAGTCACAGTTGAAGATCTTGATCCGTCCCATGTATTCCAACCCTCCC
CTCAATGGGGCCCGGATTGCTGCTGCCATTCTGAACACCCCAGATTTGCGAAAACAATGG
CTGCAAGAAGTGAAAGGCATGGCTGACCGCATCATTGGCATGCGGACTCAACTGGTCTCC
AACCTCAAGAAGGAGGGTTCCACCCACAATTGGCAACACATCACCGACCAAATTGGCATG
TTCTGTTTCACAGGGCTAAAGCCTGAACAGGTGGAGCGGCTGATCAAGGAGTTCTCCATC
TACATGACAAAAGATGGCCGCATCTCTGTGGCAGGGGTCACCTCCAGCAACGTGGGCTAC
CTTGCCCATGCCATTCACCAGGTCACCAAGTAA

1. Pol S, Bousquet-Lemercier B, Pave-Preux M, Pawlak A, Nalpas B, Berthelot P, Hanoune J, Barouki R: Nucleotide sequence and tissue distribution of the human mitochondrial aspartate aminotransferase mRNA. Biochem Biophys Res Commun. 1988 Dec 30;157(3):1309-15. [PubMed ]
2. Martini F, Angelaccio S, Barra D, Pascarella S, Maras B, Doonan S, Bossa F: The primary structure of mitochondrial aspartate aminotransferase from human heart. Biochim Biophys Acta. 1985 Nov 8;832(1):46-51. [PubMed ]

1. BCAT(c
2. ECA39 protein

MKDCSNGCSAECTGEGGSKEVVGTFKAKDLIVTPATILKEKPDPNNLVFGTVFTDHMLTV
EWSSEFGWEKPHIKPLQNLSLHPGSSALHYAVELFEGLKAFRGVDNKIRLFQPNLNMDRM
YRSAVRATLPVFDKEELLECIQQLVKLDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPTK
ALLFVLLSPVGPYFSSGTFNPVSLWANPKYVRAWKGGTGDCKMGGNYGSSLFAQCEAVDN
GCQQVLWLYGEDHQITEVGTMNLFLYWINEDGEEELATPPLDGIILPGVTRRCILDLAHQ
WGEFKVSERYLTMDDLSTALEGNRVREMFGSGTACVVCPVSDILYKGETIHIPTMENGPK
LASRILSKLTDIQYGREESDWTIVLS

• Pantothenate and CoA Biosynthesis (map00770 )
• Valine, Leucine and Isoleucine Degradation (map00280 )

• L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate

• Aminotran_4 (PF01063 )

• None

• None

ATGGATTGCAGTAACGGATCGGCAGAGTGTACCGGAGAAGGAGGATCAAAAGAGGTGGTG
GGGACTTTTAAGGCTAAAGACCTAATAGTCACACCAGCTACCATTTTAAAGGAAAAACCA
GACCCCAATAATCTGGTTTTTGGAACTGTGTTCACGGATCATATGCTGACGGTGGAGTGG
TCCTCAGAGTTTGGATGGGAGAAACCTCATATCAAGCCTCTTCAGAACCTGTCATTGCAC
CCTGGCTCATCAGCTTTGCACTATGCAGTGGAATTATTTGAAGGATTGAAGGCATTTCGA
GGAGTAGATAATAAAATTCGACTGTTTCAGCCAAACCTCAACATGGATAGAATGTATCGC
TCTGCTGTGAGGGCAACTCTGCCGGTATTTGACAAAGAAGAGCTCTTAGAGTGTATTCAA
CAGCTTGTGAAATTGGATCAAGAATGGGTCCCATATTCAACATCTGCTAGTCTGTATATT
CGTCCTGCATTCATTGGAACTGAGCCTTCTCTTGGAGTCAAGAAGCCTACCAAAGCCCTG
CTCTTTGTACTCTTGAGCCCAGTGGGACCTTATTTTTCAAGTGGAACCTTTAATCCAGTG
TCCCTGTGGGCCAATCCCAAGTATGTAAGAGCCTGGAAAGGTGGAACTGGGGACTGCAAG
ATGGGAGGGAATTACGGCTCATCTCTTTTTGCCCAATGTGAAGACGTAGATAATGGGTGT
CAGCAGGTCCTGTGGCTCTATGGCAGAGACCATCAGATCACTGAAGTGGGAACTATGAAT
CTTTTTCTTTACTGGATAAATGAAGATGGAGAAGAAGAACTGGCAACTCCTCCACTAGAT
GGCATCATTCTTCCAGGAGTGACAAGGCGGTGCATTCTGGACCTGGCACATCAGTGGGGT
GAATTTAAGGTGTCAGAGAGATACCTCACCATGGATGACTTGACAACAGCCCTGGAGGGG
AACAGAGTGAGAGAGATGTTTAGCTCTGGTACAGCCTGTGTTGTTTGCCCAGTTTCTGAT
ATACTGTACAAAGGCGAGACAATACACATTCCAACTATGGAGAATGGTCCTAAGCTGGCA
AGCCGCATCTTGAGCAAATTAACTGATATCCAGTATGGAAGAGAAGAGAGCGACTGGACA
ATTGTGCTATCCTGA

1. Schuldiner O, Eden A, Ben-Yosef T, Yanuka O, Simchen G, Benvenisty N: ECA39, a conserved gene regulated by c-Myc in mice, is involved in G1/S cell cycle regulation in yeast. Proc Natl Acad Sci U S A. 1996 Jul 9;93(14):7143-8. [PubMed ]

1. (R-3-amino-2-methylpropionate--pyruvate transaminase
2. AGT 2
3. Beta-alanine-pyruvate aminotransferase
4. Beta- ALAAT II
5. D-AIBAT

MTLIWRHLLRPLCLVTSAPRILEMHPFLSLGTSRTSVTKLSLHTKPRMPPCDFMPERYQS
LGYNRVLEIHKEHLSPVVTAYFQKPLLLHQGHMEWLFDAEGSRYLDFFSGIVTVSVGHCH
PKVNAVAQKQLGRLWHTSTVFFHPPMHEYAEKLAALLPEPLKVIFLVNSGSEANELAMLM
ARAHSNNIDIISFRGAYHGCSPYTLGLTNVGTYKMELPGGTGCQPTMCPDVFRGPWGGSH
CRDSPVQTIRKCSCAPDCCQAKDQYIEQFKDTLSTSVAKSIAGFFAEPIQGVNGVVQYPK
GFLKEAFELVRARGGVCIADEVQTGFGRLGSHFWGFQTHDVLPDIVTMAKGIGNGFPMAA
VITTPEIAKSLAKCLQHFNTFGGNPMACAIGSAVLEVIKEENLQENSQEVGTYMLLKFAK
LRDEFEIVGDVRGKGLMIGIEMVQDKISCRPLPREEVNQIHEDCKHMGLLVGRGSIFSQT
FRIAPSMCITKPEVDFAVEVFRSALTQHMERRAK

• Glycine, Serine and Threonine Metabolism (map00260 )

• L-alanine + glyoxylate = pyruvate + glycine

• Aminotran_3 (PF00202 )

• 1-24

ATGACTCTAATCTGGAGACATTTGCTGAGACCCTTGTGCCTGGTCACTTCCGCTCCCAGG
ATCCTTGAGATGCATCCTTTCCTGAGCCTAGGTACTTCCCGGACATCAGTAACCAAGCTC
AGTCTTCATACAAAGCCCAGAATGCCTCCATGTGACTTCATGCCTGAAAGATACCAGTCC
CTTGGCTACAACCGTGTCCTGGAAATCCACAAGGAACATCTTTCTCCTGTGGTGACGGCA
TATTTCCAGAAACCCCTGCTGCTCCACCAGGGGCACATGGAGTGGCTCTTTGATGCTGAA
GGAAGCAGATACCTGGATTTCTTTTCCGGGATTGTTACTGTCAGTGTTGGCCATTGCCAC
CCAAAGGTGAATGCAGTGGCACAAAAGCAGCTCGGCCGCCTGTGGCATACAAGCACCGTC
TTCTTCCACCCTCCAATGCATGAATATGCAGAGAAGCTTGCCGCACTTCTTCCTGAGCCT
CTTAAGGTCATTTTCTTGGTGAACAGTGGCTCAGAAGCCAATGAGCTGGCCATGCTGATG
GCCAGGGCGCACTCAAACAACATAGACATCATTTCTTTCAGAGGAGCCTACCATGGATGC
AGTCCTTACACACTTGGCTTGACAAACGTAGGGACCTACAAGATGGAACTCCCTGGTGGG
ACAGGTTGCCAACCAACAATGTGTCCAGATGTTTTTCGTGGCCCTTGGGGAGGAAGCCAC
TGTCGAGATTCTCCAGTGCAAACAATCAGGAAGTGCAGCTGTGCACCAGACTGCTGCCAA
GCTAAAGATCAGTATATTGAGCAATTCAAAGATACGCTGAGCACATCTGTGGCCAAGTCA
ATTGCTGGATTTTTCGCAGAACCTATTCAAGGTGTGAATGGAGTTGTCCAGTACCCAAAG
GGGTTTCTAAAGGAAGCCTTTGAGCTGGTGCGAGCAAGGGGAGGCGTGTGCATTGCAGAT
GAAGTGCAGACAGGATTTGGAAGGTTGGGCTCTCACTTCTGGGGCTTCCAAACCCACGAT
GTCCTGCCTGACATTGTCACCATGGCTAAAGGGATTGGGAATGGCTTTCCCATGGCAGCA
GTCATAACCACTCCAGAGATTGCCAAATCTTTGGCGAAATGCCTGCAGCACTTCAACACC
TTTGGAGGGAACCCCATGGCCTGTGCCATTGGATCTGCTGTGCTTGAGGTGATTAAAGAA
GAAAATCTACAGGAAAACAGTCAAGAAGTTGGGACCTACATGTTACTAAAGTTTGCTAAG
CTGCGGGATGAATTTGAAATTGTTGGAGACGTCCGAGGCAAAGGTCTCATGATAGGCATA
GAAATGGTGCAGGATAAGATAAGCTGTCGGCCTCTTCCCCGTGAAGAAGTAAATCAGATC
CATGAGGACTGCAAGCACATGGGACTCCTCGTTGGCAGAGGCAGCATTTTTTCTCAGACA
TTTCGCATTGCGCCCTCAATGTGCATCACTAAACCAGAAGTTGATTTTGCAGTAGAAGTA
TTTCGTTCTGCCTTAACCCAACACATGGAAAGAAGAGCTAAGTAA

1. Ornithine--oxo-acid aminotransferase[Contains: Ornithine aminotransferase, hepatic form
2. Ornithine aminotransferase, renal form]

MFSKLAHLQRFAVLSRGVHSSVASATSVATKKTVQGPPTSDDIFEREYKYGAHNYHPLPV
ALERGKGIYLWDVEGRKYFDFLSSYSAVNQGHCHPKIVNALKSQVDKLTLTSRAFYNNVL
GEYEEYITKLFNYHKVLPMNTGVEAGETACKLARKWGYTVKGIQKYKAKIVFAAGNFWGR
TLSAISSSTDPTSYDGFGPFMPGFDIIPYNDLPALERALQDPNVAAFMVEPIQGEAGVVV
PDPGYLMGVRELCTRHQVLFIADEIQTGLARTGRWLAVDYENVRPDIVLLGKALSGGLYP
VSAVLCDDDIMLTIKPGEHGSTYGGNPLGCRVAIAALEVLEEENLAENADKLGIILRNEL
MKLPSDVVTAVRGKGLLNAIVIKETKDWDAWKVCLRLRDNGLLAKPTHGDIIRFAPPLVI
KEDELRESIEIINKTILSF

• Arginine and Proline Metabolism (map00330 )

• L-ornithine + a 2-oxo acid = L-glutamate 5-semialdehyde + an L-amino acid

• Aminotran_3 (PF00202 )

• 1-20

ATGTTTTCCAAACTAGCACATTTGCAGAGGTTTGCTGTACTTAGTCGCGGAGTTCATTCT
TCAGTGGCTTCTGCTACATCTGTTGCAACTAAAAAAACAGTCCAAGGCCCTCCAACCTCT
GATGACATTTTTGAAAGGGAATATAAGTATGGTGCACACAACTACCATCCTTTACCTGTA
GCCCTGGAGAGAGGAAAAGGTATTTACTTATGGGATGTAGAAGGCAGAAAATATTTTGAC
TTCCTGAGTTCTTACAGTGCTGTCAACCAAGGGCATTGTCACCCCAAGATTGTGAATGCT
CTGAAGAGTCAAGTGGACAAATTGACCTTAACATCTAGAGCTTTCTATAATAACGTACTT
GGTGAATATGAGGAGTATATTACTAAACTTTTCAACTACCACAAAGTTCTTCCTATGAAT
ACAGGAGTGGAGGCTGGAGAGACTGCCTGTAAACTAGCTCGTAAGTGGGGCTATACCGTG
AAGGGCATTCAGAAATACAAAGCAAAGATTGTTTTTGCAGCTGGGAACTTCTGGGGTAGG
ACGTTGTCTGCTATCTCCAGTTCCACAGACCCAACCAGTTACGATGGTTTTGGACCATTT
ATGCCGGGATTCGACATCATTCCCTATAATGATCTGCCCGCACTGGAGCGTGCTCTTCAG
GATCCAAATGTGGCTGCGTTCATGGTAGAACCAATTCAGGGTGAAGCAGGCGTTGTTGTT
CCGGATCCAGGTTACCTAATGGGAGTGCGAGAGCTCTGCACCAGGCACCAGGTTCTCTTT
ATTGCTGATGAAATACAGACAGGATTGGCCAGAACTGGTAGATGGCTGGCTGTTGATTAT
GAAAATGTCAGACCTGATATAGTCCTCCTTGGAAAGGCCCTTTCTGGGGGCTTATACCCT
GTGTCTGCAGTGCTGTGTGATGATGACATCATGCTGACCATTAAGCCAGGGGAGCATGGG
TCCACATACGGTGGCAATCCACTAGGCTGCCGAGTGGCCATCGCAGCCCTTGAGGTTTTA
GAAGAAGAAAACCTTGCTGAAAATGCAGACAAATTGGGCATTATCTTGAGAAATGAACTC
ATGAAGCTACCTTCTGATGTTGTAACTGCCGTAAGAGGAAAAGGATTATTAAACGCTATT
GTCATTAAAGAAACCAAAGATTGGGATGCTTGGAAGGTGTGTCTACGACTTCGAGATAAT
GGACTTCTGGCCAAGCCAACCCATGGCGACATTATCAGGTTTGCGCCTCCGCTGGTGATC
AAGGAGGATGAGCTTCGAGAGTCCATTGAAATTATTAACAAGACCATCTTGTCTTTCTGA

1. Inana G, Totsuka S, Redmond M, Dougherty T, Nagle J, Shiono T, Ohura T, Kominami E, Katunuma N: Molecular cloning of human ornithine aminotransferase mRNA. Proc Natl Acad Sci U S A. 1986 Mar;83(5):1203-7. [PubMed ]
2. Ramesh V, Shaffer MM, Allaire JM, Shih VE, Gusella JF: Investigation of gyrate atrophy using a cDNA clone for human ornithine aminotransferase. DNA. 1986 Dec;5(6):493-501. [PubMed ]
3. Kobayashi T, Nishii M, Takagi Y, Titani K, Matsuzawa T: Molecular cloning and nucleotide sequence analysis of mRNA for human kidney ornithine aminotransferase. An examination of ornithine aminotransferase isozymes between liver and kidney. FEBS Lett. 1989 Sep 25;255(2):300-4. [PubMed ]
4. Mitchell GA, Looney JE, Brody LC, Steel G, Suchanek M, Engelhardt JF, Willard HF, Valle D: Human ornithine-delta-aminotransferase. cDNA cloning and analysis of the structural gene. J Biol Chem. 1988 Oct 5;263(28):14288-95. [PubMed ]
5. Zintz CB, Inana G: Analysis of the human ornithine aminotransferase gene family. Exp Eye Res. 1990 Jun;50(6):759-70. [PubMed ]
6. Ramesh V, Gusella JF, Shih VE: Molecular pathology of gyrate atrophy of the choroid and retina due to ornithine aminotransferase deficiency. Mol Biol Med. 1991 Feb;8(1):81-93. [PubMed ]
7. Simmaco M, John RA, Barra D, Bossa F: The primary structure of ornithine aminotransferase. Identification of active-site sequence and site of post-translational proteolysis. FEBS Lett. 1986 Apr 7;199(1):39-42. [PubMed ]
8. Shah SA, Shen BW, Brunger AT: Human ornithine aminotransferase complexed with L-canaline and gabaculine: structural basis for substrate recognition. Structure. 1997 Aug 15;5(8):1067-75. [PubMed ]
9. Shen BW, Hennig M, Hohenester E, Jansonius JN, Schirmer T: Crystal structure of human recombinant ornithine aminotransferase. J Mol Biol. 1998 Mar 20;277(1):81-102. [PubMed ]
10. Storici P, Capitani G, Muller R, Schirmer T, Jansonius JN: Crystal structure of human ornithine aminotransferase complexed with the highly specific and potent inhibitor 5-fluoromethylornithine. J Mol Biol. 1999 Jan 8;285(1):297-309. [PubMed ]
11. Ramesh V, McClatchey AI, Ramesh N, Benoit LA, Berson EL, Shih VE, Gusella JF: Molecular basis of ornithine aminotransferase deficiency in B-6-responsive and -nonresponsive forms of gyrate atrophy. Proc Natl Acad Sci U S A. 1988 Jun;85(11):3777-80. [PubMed ]
12. Inana G, Chambers C, Hotta Y, Inouye L, Filpula D, Pulford S, Shiono T: Point mutation affecting processing of the ornithine aminotransferase precursor protein in gyrate atrophy. J Biol Chem. 1989 Oct 15;264(29):17432-6. [PubMed ]
13. Michaud J, Brody LC, Steel G, Fontaine G, Martin LS, Valle D, Mitchell G: Strand-separating conformational polymorphism analysis: efficacy of detection of point mutations in the human ornithine delta-aminotransferase gene. Genomics. 1992 Jun;13(2):389-94. [PubMed ]
14. Brody LC, Mitchell GA, Obie C, Michaud J, Steel G, Fontaine G, Robert MF, Sipila I, Kaiser-Kupfer M, Valle D: Ornithine delta-aminotransferase mutations in gyrate atrophy. Allelic heterogeneity and functional consequences. J Biol Chem. 1992 Feb 15;267(5):3302-7. [PubMed ]
15. Michaud J, Thompson GN, Brody LC, Steel G, Obie C, Fontaine G, Schappert K, Keith CG, Valle D, Mitchell GA: Pyridoxine-responsive gyrate atrophy of the choroid and retina: clinical and biochemical correlates of the mutation A226V. Am J Hum Genet. 1995 Mar;56(3):616-22. [PubMed ]
16. Kobayashi T, Ogawa H, Kasahara M, Shiozawa Z, Matsuzawa T: A single amino acid substitution within the mature sequence of ornithine aminotransferase obstructs mitochondrial entry of the precursor. Am J Hum Genet. 1995 Aug;57(2):284-91. [PubMed ]

1. Gamma- glutamylcysteine synthetase
2. Gamma-ECS
3. GCS heavy chain

MGLLSQGSPLSWEETKRHADHVRRHGILQFLHIYHAVKDRHKDVLKWGDEVEYMLVSFDH
ENKKVRLVLSGEKVLETLQEKGERTNPNHPTLWRPEYGSYMIEGTPGQPYGGTMSEFNTV
EANMRKRRKEATSILEENQALCTITSFPRLGCPGFTLPEVKPNPVEGGASKSLFFPDEAI
NKHPRFSTLTRNIRHRRGEKVVINVPIFKDKNTPSPFIETFTEDDEASRASKPDHIYMDA
MGFGMGNCCLQVTFQACSISEARYLYDQLATICPIVMALSAASPFYRGYVSDIDCRWGVI
SASVDDRTREERGLEPLKNNNYRISKSRYDSIDSYLSKCGEKYNDIDLTIDKEIYEQLLQ
EGIDHLLAQHVAHLFIRDPLTLFEEKIHLDDANESDHFENIQSTNWQTMRFKPPPPNSDI
GWRVEFRPMEVQLTDFENSAYVVFVVLLTRVILSYKLDFLIPLSKVDENMKVAQKRDAVL
QGMFYFRKDICKGGNAVVDGCGKAQNSTELAAEEYTLMSIDTIINGKEGVFPGLIPILNS
YLENMEVDVDTRCSILNYLKLIKKRASGELMTVARWMREFIANHPDYKQDSVITDEMNYS
LILKCNQIANELCECPELLGSAFRKVKYSGSKTDSSN

• Glutamate Metabolism (map00251 )
• Glutathione Metabolism (map00480 )

• ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine

• GCS (PF03074 )

• None

• None

ATGGGGCTGCTGTCCCAGGGCTCGCCGCTGAGCTGGGAGGAAACCAAGCGCCATGCCGAC
CACGTGCGGCGGCACGGGATCCTCCAGTTCCTGCACATCTACCACGCCGTCAAGGACCGG
CACAAGGACGTTCTCAAGTGGGGCGATGAGGTGGAATACATGTTGGTATCTTTTGATCAT
GAAAATAAAAAAGTCCGGTTGGTCCTGTCTGGGGAGAAAGTTCTTGAAACTCTGCAAGAG
AAGGGGGAAAGGACAAACCCAAACCATCCTACCCTTTGGAGACCAGAGTATGGGAGTTAC
ATGATTGAAGGGACACCAGGACAGCCCTACGGAGGAACAATGTCCGAGTTCAATACAGTT
GAGGCCAACATGCGAAAACGCCGGAAGGAGGCTACTTCTATATTAGAAGAAAATCAGGCT
CTTTGCACAATAACTTCATTTCCCAGATTAGGCTGTCCTGGGTTCACACTGCCCGAGGTC
AAACCCAACCCAGTGGAAGGAGGAGCTTCCAAGTCCCTCTTCTTTCCAGATGAAGCAATA
AACAAGCACCCTCGCTTCAGTACCTTAACAAGAAATATCCGACATAGGAGAGGAGAAAAG
GTTGTCATCAATGTACCAATATTTAAGGACAAGAATACACCATCTCCATTTATAGAAACA
TTTACTGAGGATGATGAAGCTTCAAGGGCTTCTAAGCCGGATCATATTTACATGGATGCC
ATGGGATTTGGAATGGGCAATTGCTGTCTCCAGGTGACATTCCAAGCCTGCAGTATATCT
GAGGCCAGATACCTTTATGATCAGTTGGCTACTATCTGTCCAATTGTTATGGCTTTGAGT
GCTGCATCTCCCTTTTACCGAGGCTATGTGTCAGACATTGATTGTCGCTGGGGAGTGATT
TCTGCATCTGTAGATGATAGAACTCGGGAGGAGCGAGGACTGGAGCCATTGAAGAACAAT
AACTATAGGATCAGTAAATCCCGATATGACTCAATAGACAGCTATTTATCTAAGTGTGGT
GAGAAATATAATGACATCGACTTGACGATAGATAAAGAGATCTACGAACAGCTGTTGCAG
GAAGGCATTGATCATCTCCTGGCCCAGCATGTTGCTCATCTCTTTATTAGAGACCCACTG
ACACTGTTTGAAGAGAAAATACACCTGGATGATGCTAATGAGTCTGACCATTTTGAGAAT
ATTCAGTCCACAAATTGGCAGACAATGAGATTTAAGCCCCCTCCTCCAAACTCAGACATT
GGATGGAGAGTAGAATTTCGACCCATGGAGGTGCAATTAACAGACTTTGAGAACTCTGCC
TATGTGGTGTTTGTGGTACTGCTCACCAGAGTGATCCTTTCCTACAAATTGGATTTTCTC
ATTCCACTGTCAAAGGTTGATGAGAACATGAAGGTAGCACAGAAAAGAGATGCTGTCTTG
CAGGGAATGTTTTATTTCAGGAAAGATATTTGCAAAGGTGGCAATGCAGTGGTGGATGGT
TGTGGCAAGGCCCAGAACAGCACGGAGCTCGCTGCAGAGGAGTACACCCTCATGAGCATA
GACACCATCATCAATGGGAAGGAAGGTGTGTTTCCTGGACTGATCCCAATTCTGAACTCT
TACCTTGAAAACATGGAAGTGGATGTGGACACCAGATGTAGTATTCTGAACTACCTAAAG
CTAATTAAGAAGAGAGCATCTGGAGAACTAATGACAGTTGCCAGATGGATGAGGGAGTTT
ATCGCAAACCATCCTGACTACAAGCAAGACAGTGTCATAACTGATGAAATGAATTATAGC
CTTATTTTGAAGTGTAACCAAATTGCAAATGAATTATGTGAATGCCCAGAGTTACTTGGA
TCAGCATTTAGGAAAGTAAAATATAGTGGAAGTAAAACTGACTCATCCAACTAG

1. Gipp JJ, Chang C, Mulcahy RT: Cloning and nucleotide sequence of a full-length cDNA for human liver gamma-glutamylcysteine synthetase. Biochem Biophys Res Commun. 1992 May 29;185(1):29-35. [PubMed ]
2. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed ]
3. Mulcahy RT, Gipp JJ: Identification of a putative antioxidant response element in the 5'-flanking region of the human gamma-glutamylcysteine synthetase heavy subunit gene. Biochem Biophys Res Commun. 1995 Apr 6;209(1):227-33. [PubMed ]
4. Beutler E, Gelbart T, Kondo T, Matsunaga AT: The molecular basis of a case of gamma-glutamylcysteine synthetase deficiency. Blood. 1999 Oct 15;94(8):2890-4. [PubMed ]
5. Ristoff E, Augustson C, Geissler J, de Rijk T, Carlsson K, Luo JL, Andersson K, Weening RS, van Zwieten R, Larsson A, Roos D: A missense mutation in the heavy subunit of gamma-glutamylcysteine synthetase gene causes hemolytic anemia. Blood. 2000 Apr 1;95(7):2193-6. [PubMed ]

1. Amino-acid acetyltransferase[Contains: N-acetylglutamate synthase long form
2. N-acetylglutamate synthase short form
3. N-acetylglutamate synthase conserved domain form]

MATALMAVVLRAAAVAPRLRGRGGTGGARRLSCGARRRAARGTSPGRRLSTAWSQPQPPP
EEYAGADDVSQSPVAEEPSWVPSPRPPVPHESPEPPSGRSLVQRDIQAFLNQCGASPGEA
RHWLTQFQTCHHSADKPFAVIEVDEEVLKCQQGVSSLAFALAFLQRMDMKPLVVLGLPAP
TAPSGCLSFWEAKAQLAKSCKVLVDALRHNAAAAVPFFGGGSVLRAAEPAPHASYGGIVS
VETDLLQWCLESGSIPILCPIGETAARRSVLLDSLEVTASLAKALRPTKIIFLNNTGGLR
DSSHKVLSNVNLPADLDLVCNAEWVSTKERQQMRLIVDVLSRLPHHSSAVITAASTLLTE
LFSNKGSGTLFKNAERMLRVRSLDKLDQGRLVDLVNASFGKKLRDDYLASLRPRLHSIYV
SEGYNAAAILTMEPVLGGTPYLDKFVVSSSRQGQGSGQMLWECLRRDLQTLFWRSRVTNP
INPWYFKHSDGSFSNKQWIFFWFGLADIRDSYELVNHAKGLPDSFHKPASDPGS

• acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate

• DUF619 (PF04768 )

• 1-21

ATGGCGACGGCGCTGATGGCTGTGGTTCTGCGGGCAGCTGCTGTAGCCCCGAGGCTGAGA
GGCCGGGGAGGCACTGGGGGCGCCCGAAGGCTGAGCTGTGGCGCGCGGCGGCGGGCGGCG
AGGGGCACCAGCCCGGGGCGCCGGCTCAGCACCGCCTGGTCGCAGCCCCAGCCCCCGCCC
GAGGAGTACGCGGGCGCGGACGACGTCTCCCAGTCGCCCGTCGCCGAGGAGCCGTCGTGG
GTGCCGAGTCCCAGGCCCCCGGTGCCCCACGAGTCCCCAGAGCCTCCTTCGGGCCGCTCG
CTGGTGCAGCGGGACATCCAGGCCTTCCTGAACCAGTGCGGGGCCAGCCCTGGGGAGGCG
CGCCACTGGCTCACGCAGTTCCAGACCTGCCATCACTCCGCGGACAAGCCCTTCGCCGTC
ATCGAGGTGGACGAGGAGGTGCTCAAGTGCCAGCAGGGCGTATCCAGTCTGGCCTTTGCC
CTGGCCTTCTTGCAGCGCATGGACATGAAGCCGCTGGTGGTCCTGGGGCTGCCGGCCCCT
ACGGCTCCCTCGGGCTGTCTTTCCTTCTGGGAGGCCAAGGCGCAGCTGGCCAAGAGCTGC
AAGGTGCTGGTAGACGCGCTTCGACACAACGCCGCCGCTGCTGTGCCATTTTTTGGCGGC
GGGTCTGTGCTACGCGCTGCCGAGCCGGCTCCCCATGCCAGCTACGGCGGCATCGTCTCG
GTGGAGACAGACCTGCTGCAGTGGTGCCTGGAGTCGGGCAGCATCCCCATCCTGTGCCCC
ATCGGGGAGACGGCCGCGCGCCGCTCCGTGCTTCTCGACTCCCTGGAGGTGACCGCGTCG
CTGGCCAAGGCGCTGCGGCCCACCAAAATCATCTTCCTCAATAACACAGGCGGCCTGCGC
GACAGCAGTCATAAGGTCCTGAGTAACGTGAACCTGCCCGCCGACCTGGACCTGGTGTGC
AACGCCGAGTGGGTGAGCACAAAAGAACGGCAGCAGATGCGGCTCATCGTGGACGTGCTC
AGCCGCCTGCCCCACCACTCCTCGGCCGTCATCACCGCCGCTAGCACGCTGCTCACTGAG
CTCTTTAGCAACAAGGGGTCCGGGACCCTGTTCAAGAACGCCGAGCGAATGCTACGGGTG
CGCAGCCTGGACAAGCTGGACCAGGGCCGTCTAGTGGACCTGGTCAACGCCAGCTTCGGC
AAGAAGCTCAGGGACGACTACCTGGCCTCGCTGCGCCCGCGGCTGCACTCCATCTACGTC
TCCGAGGGGTACAACGCCGCCGCCATTCTGACCATGGAGCCCGTCCTGGGGGGCACCCCG
TACCTGGACAAATTTGTGGTGAGCTCCAGCCGCCAGGGCCAAGGCTCCGGCCAGATGCTG
TGGGAGTGCCTGCGGCGGGACCTTCAGACACTTTTCTGGCGCTCCCGGGTCACCAACCCC
ATCAATCCCTGGTACTTCAAACACAGTGATGGCAGCTTCTCCAACAAGCAGTGGATCTTC
TTCTGGTTTGGCCTGGCTGATATCCGGGACTCCTATGAGTTGGTCAACCACGCCAAGGGA
CTGCCAGACTCCTTTCACAAGCCAGCTTCTGACCCAGGCAGCTGA

1. Haberle J, Schmidt E, Pauli S, Kreuder JG, Plecko B, Galler A, Wermuth B, Harms E, Koch HG: Mutation analysis in patients with N-acetylglutamate synthase deficiency. Hum Mutat. 2003 Jun;21(6):593-7. [PubMed ]
2. Caldovic L, Morizono H, Gracia Panglao M, Gallegos R, Yu X, Shi D, Malamy MH, Allewell NM, Tuchman M: Cloning and expression of the human N-acetylglutamate synthase gene. Biochem Biophys Res Commun. 2002 Dec 13;299(4):581-6. [PubMed ]

1. BCAT(m
2. Placental protein 18
3. PP18

MAAAALGQIWARKLLSVPWLLCGPRRYASSSFKAADLQLEMTQKPHKKPGPGEPLVFGKT
FTDHMLMVEWNDKGWGQPRIQPFQNLTLHPASSSLHYSLQLFEGMKAFKGKDQQVRLFRP
WLNMDRMLRSAMRLCLPSFDKLELLECIRRLIEVDKDWVPDAAGTSLYVRPVLIGNEPSL
GVSQPTRALLFVILCPVGAYFPGGSVTPVSLLADPAFIRAWVGGVGNYKLGGNYGPTVLV
QQEALKRGCEQVLWLYGPDHQLTEVGTMNIFVYWTHEDGVLELVTPPLNGVILPGVVRQS
LLDMAQTWGEFRVVERTITMKQLLRALEEGRVREVFGSGTACQVCPVHRILYKDRNLHIP
TMENGPELILRFQKELKEIQYGIRAHEWMFPV

• Pantothenate and CoA Biosynthesis (map00770 )
• Valine, Leucine and Isoleucine Degradation (map00280 )

• L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate

• Aminotran_4 (PF01063 )

• 1-29

ATGGCCGCAGCCGCTCTGGGGCAGATCTGGGCACGAAAGCTTCTCTCTGTCCCTTGGCTT
CTGTGTGGTCCCAGAAGATATGCCTCCTCCAGTTTCAAGGCTGCAGACCTGCAGCTGGAA
ATGACACAGAAGCCTCATAAGAAGCCTGGCCCCGGCGAGCCCCTGGTGTTTGGGAAGACA
TTTACCGACCACATGCTGATGGTGGAATGGAATGACAAGGGCTGGGGCCAGCCCCGAATC
CAGCCCTTCCAGAACCTCACGCTGCACCCAGCCTCCTCCAGCCTCCACTACTCCCTGCAG
CTGTTTGAGGGCATGAAGGCGTTCAAAGGCAAAGACCAGCAGGTGCGCCTCTTCCGCCCC
TGGCTCAACATGGACCGGATGCTGCGCTCAGCCATGCGCCTGTGCCTGCCGAGTTTCGAC
AAGCTGGAGTTGCTGGAGTGCATCCGCCGGCTCATCGAAGTGGACAAGGACTGGGTCCCC
GATGCCGCCGGCACCAGCCTCTATGTGCGGCCTGTGCTCATTGGGAACGAGCCCTCGCTG
GGTGTCAGCCAGCCCAGGCGCGCGCTCCTGTTCGTCATTCTCTGCCCAGTGGGTGCCTAC
TTCCCTGGAGGCTCCGTGACCCCGGTCTCCCTCCTGGCCGACCCAGCCTTCATCCGGGCC
TGGGTGGGCGGGGTCGGCAACTACAAGTTAGGTGGGAATTATGGGCCCACCGTGTTAGTG
CAACAGGAGGCACTCAAGCGGGGCTGTGAACAGGTCCTCTGGCTGTATGGGCCCGACCAC
CAGCTCACCGAGGTGGGAACCATGAACATCTTTGTCTACTGGACCCACGAAGATGGGGTG
CTGGAGCTGGTGACGCCCCCGCTGAATGGTGTTATCCTGCCTGGAGTGGTCAGACAGAGT
CTACTGGACATGGCTCAGACCTGGGGTGAGTTCCGGGTGGTGGAGCGCACGATCACCATG
AAGCAGTTGCTGCGGGCCTTGGAGGAGGGCCGCGTGCGGGAAGTCTTTGGCTCGGGCACC
GCTTGCCAGGTCTGCCCAGTGCACCGAATCCTGTACAAAGACAGGAACCTCCATATTCCC
ACCATGGAAAATGGGCCTGAGCTGATCCTCCGCTTCCAGAAGGAGCTGAAGGAGATCCAG
TACGGAATCAGAGCCCACGAGTGGATGTTCCCGGTGTGA

1. Bledsoe RK, Dawson PA, Hutson SM: Cloning of the rat and human mitochondrial branched chain aminotransferases (BCATm). Biochim Biophys Acta. 1997 Apr 25;1339(1):9-13. [PubMed ]
2. Than NG, Sumegi B, Than GN, Bellyei S, Bohn H: Molecular cloning and characterization of placental tissue protein 18 (PP18a)/human mitochondrial branched-chain aminotransferase (BCATm) and its novel alternatively spliced PP18b variant. Placenta. 2001 Feb-Mar;22(2-3):235-43. [PubMed ]
3. Eden A, Simchen G, Benvenisty N: Two yeast homologs of ECA39, a target for c-Myc regulation, code for cytosolic and mitochondrial branched-chain amino acid aminotransferases. J Biol Chem. 1996 Aug 23;271(34):20242-5. [PubMed ]
4. Yennawar N, Dunbar J, Conway M, Hutson S, Farber G: The structure of human mitochondrial branched-chain aminotransferase. Acta Crystallogr D Biol Crystallogr. 2001 Apr;57(Pt 4):506-15. [PubMed ]
5. Yennawar NH, Conway ME, Yennawar HP, Farber GK, Hutson SM: Crystal structures of human mitochondrial branched chain aminotransferase reaction intermediates: ketimine and pyridoxamine phosphate forms. Biochemistry. 2002 Oct 1;41(39):11592-601. [PubMed ]

1. Glutamate--tRNA ligase
2. Prolyl-tRNA synthetase
3. Proline--tRNA ligase]

MEHTEIDHWLEFSATKLSSCDSFTSTINELNHCLSLRTYLVGNSLSLADLCVWATLKGNA
AWQEQLKQKKAPVHVKRWFGFLEAQQAFQSVGTKWDVSTTKARVAPEKKQDVGKFVELPG
AEMGKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVI
LEDVAMLHIKPDQFTYTSDHFETIMKYAEKLIQEGKAYVDDTPAEQMKAEREQRIESKHR
KNPIEKNLQMWEEMKKGSQFGHSCCLRAKIDMSSNNGCMRDPTLYRCKIQPHPRTGNKYN
VYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIRKPYIWEYSRLNLNNTV
LSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKI
WAFNKKVIDPVAPRYVALLKKEVIPVNVPEAQEEMKEVAKHPKNPEVGLKPVWYSPKVFI
EGADAETFSEGEMVTFINWGNLNITKIHKNADGKIISLDAKFNLENKDYKKTTKVTWLAE
TTHALPIPVICVTYEHLITKPVLGKDEDFKQYVNKNSKHEELMLGDPCLKDLKKGDIIQL
QRRGFFICDQPYEPVSPYSCKEAPCVLIYIPDGHTKEMPTSGSKEKTKVEATKNETSAPF
KERPTPSLNNNCTTSEDSLVLYNRVAVQGDVVRELKAKKAPKEDVDAAVKQLLSLKAEYK
EKTGQEYKPGNPPAEIGQNISSNSSASILESKSLYDEVAAQGEVVRKLKAEKSPKAKINE
AVECLLSLKAQYKEKTGKEYIPGQPPLSQSSDSSPTRNSEPAGLETPEAKVLFDKVASQG
EVVRKLKTEKAPKDQVDIAVQELLQLKAQYKSLIGVEYKPVSATGAEDKDKKKKEKENKS
EKQNKPQKQNDGQRKDPSKNQGGGLSSSGAGEGQGPKKQTRLGLEAKKEENLADWYSQVI
TKSEMIEYHDISGCYILRPWAYAIWEAIKDFFDAEIKKLGVENCYFPMFVSQSALEKEKT
HVADFAPEVAWVTRSGKTELAEPIAIRPTSETVMYPAYAKWVQSHRDLPIKLNQWCNVVR
WEFKHPQPFLRTREFLWQEGHSAFATMEEAAEEVLQILDLYAQVYEELLAIPVVKGRKTE
KEKFAGGDYTTTIEAFISASGRAIQGGTSHHLGQNFSKMFEIVFEDPKIPGEKQFAYQNS
WGLTTRTIGVMTMVHGDNMGLVLPPRVACVQVVIIPCGITNALSEEDKEALIAKCNDYRR
RLLSVNIRVRADLRDNYSPGWKFNHWELKGVPIRLEVGPRDMKSCQFVAVRRDTGEKLTV
AENEAETKLQAILEDIQVTLFTRASEDLKTHMVVANTMEDFQKILDSGKIVQIPFCGEID
CEDWIKKTTARDQDLEPGAPSMGAKSLCIPFKPLCELQPGAKCVCGKNPAKYYTLFGRSY

• Aminoacyl-tRNA biosynthesis (map00970 )
• Glutamate Metabolism (map00251 )
• Porphyrin Metabolism (map00860 )

• ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu)

• HGTP_anticodon (PF03129 )
• ProRS-C_1 (PF09180 )
• tRNA-synt_1c (PF00749 )
• tRNA-synt_1c_C (PF03950 )
• tRNA-synt_2b (PF00587 )
• WHEP-TRS (PF00458 )

• None

• None

ATGGAACATACTGAGATTGATCACTGGTTGGAGTTCAGTGCTACAAAATTATCTTCATGT
GATTCCTTTACTTCTACAATTAATGAACTCAATCATTGCCTGTCTCTGAGAACATACTTA
GTTGGAAACTCCTTGAGTTTAGCAGATTTATGTGTTTGGGCCACCCTAAAAGGAAATGCT
GCCTGGCAAGAACAGTTGAAACAGAAGAAAGCTCCAGTTCATGTAAAACGTTGGTTTGGC
TTTCTTGAAGCCCAGCAGGCCTTCCAGTCAGTAGGTACCAAGTGGGATGTTTCAACAACC
AAAGCTCGAGTGGCACCTGAGAAAAAGCAAGATGTTGGGAAATTTGTTGAGCTTCCAGGT
GCGGAGATGGGAAAGGTTACCGTCAGATTTCCTCCAGAGGCCAGTGGTTACTTACACATT
GGGCATGCAAAAGCTGCTCTTCTGAACCAGCACTACCAGGTTAACTTTAAAGGGAAACTG
ATCATGAGATTTGATGACACAAATCCTGAAAAAGAAAAGGAAGATTTTGAGAAGGTTATC
TTGGAAGATGTTGCAATGTTGCATATCAAACCAGATCAATTTACTTATACTTCGGATCAT
TTTGAAACTATAATGAAGTATGCAGAGAAGCTAATTCAAGAAGGGAAGGCTTATGTGGAT
GATACTCCTGCTGAACAGATGAAAGCAGAACGTGAGCAGAGGATAGAATCTAAACATAGA
AAAAACCCTATTGAGAAGAATCTACAAATGTGGGAAGAAATGAAAAAAGGGAGCCAGTTT
GGTCACTCCTGTTGTTTGCGAGCAAAAATTGACATGAGTAGTAACAATGGATGCATGAGA
GATCCAACCCTTTATCGCTGCAAAATTCAACCACATCCAAGAACTGGAAATAAATACAAT
GTTTATCCAACATATGATTTTGCCTGCCCCATAGTTGACAGCATCGAAGGTGTTACACAT
GCCCTGAGAACAACAGAATACCATGACAGAGATGAGCAGTTTTACTGGATTATTGAAGCT
TTAGGCATAAGAAAACCATATATTTGGGAATATAGTCGGCTAAATCTCAACAACACAGTG
CTATCCAAAAGAAAACTCACATGGTTTGTCAATGAAGGACTAGTAGATGGATGGGATGAC
CCAAGATTTCCTACGGTTCGTGGTGTACTGAGAAGAGGGATGACAGTTGAAGGACTGAAA
CAGTTTATTGCTGCTCAGGGCTCCTCACGTTCAGTCGTGAACATGGAGTGGGACAAAATC
TGGGCGTTTAACAAAAAGGTTATTGACCCAGTGGCTCCACGATATGTTGCATTACTGAAG
AAAGAAGTGATCCCAGTGAATGTACCTGAAGCTCAGGAGGAGATGAAAGAAGTAGCCAAA
CACCCAAAGAATCCTGAGGTTGGCTTGAAGCCTGTGTGGTATAGTCCCAAAGTTTTCATT
GAAGGTGCTGATGCAGAGACTTTTTCGGAGGGTGAGATGGTTACATTTATAAATTGGGGC
AACCTCAACATTACAAAAATACACAAAAATGCAGATGGAAAAATCATATCTCTTGATGCA
AAGTTTAATTTGGAAAACAAAGACTACAAGAAAACCACTAAGGTCACTTGGCTTGCAGAG
ACTACACATGCTCTTCCTATTCCAGTAATCTGTGTCACTTATGAGCACTTGATCACAAAG
CCAGTGCTAGGAAAAGACGAGGACTTTAAGCAGTATGTCAACAAGAACAGTAAGCATGAA
GAGCTAATGCTAGGGGATCCCTGCCTTAAGGATTTGAAAAAAGGAGATATTATACAACTC
CAGAGAAGAGGATTCTTCATATGTGATCAACCTTATGAACCTGTTAGCCCATATAGTTGC
AAGGAAGCCCCGTGTGTTTTGATATACATTCCTGATGGGCACACAAAGGAAATGCCAACA
TCAGGGTCAAAGGAAAAGACCAAAGTAGAAGCCACAAAAAATGAGACCTCTGCTCCTTTT
AAGGAAAGACCAACACCTTCTCTGAATAATAATTGTACTACATCTGAGGATTCCTTGGTC
CTTTACAATAGAGTGGCTGTTCAAGGAGATGTGGTTCGTGAATTAAAAGCCAAGAAAGCA
CCAAAGGAAGATGTAGATGCAGCTGTAAAACAGCTTTTGTCTTTGAAAGCTGAATATAAG
GAGAAAACTGGCCAGGAATATAAACCTGGAAACCCTCCTGCTGAAATAGGACAGAATATT
TCTTCTAATTCCTCAGCAAGTATTCTGGAAAGTAAATCTCTGTATGATGAAGTTGCTGCA
CAAGGGGAGGTGGTTCGTAAGCTAAAAGCTGAAAAATCCCCTAAGGCTAAAATAAATGAA
GCTGTAGAATGCTTACTGTCCCTGAAGGCTCAGTATAAAGAAAAAACTGGGAAGGAGTAC
ATACCTGGTCAGCCCCCATTATCTCAAAGTTCGGATTCAAGCCCAACCAGAAATTCTGAA
CCTGCTGGTTTAGAAACACCAGAAGCGAAAGTACTTTTTGACAAAGTAGCTTCTCAAGGG
GAAGTAGTTCGGAAACTTAAAACTGAAAAAGCCCCTAAGGATCAAGTAGATATAGCTGTT
CAAGAACTCCTTCAGCTAAAGGCACAGTACAAGTCTTTGATAGGAGTAGAGTATAAGCCT
GTGTCGGCCACTGGAGCTGAGGACAAAGATAAGAAGAAGAAAGAAAAAGAAAATAAATCT
GAAAAGCAGAATAAGCCTCAGAAACAAAATGATGGCCAAAGGAAAGACCCTTCTAAAAAC
CAAGGAGGTGGGCTCTCATCAAGTGGAGCAGGAGAAGGGCAGGGGCCTAAGAAACAGACC
AGGTTGGGTCTTGAGGCAAAAAAAGAAGAAAATCTTGCTGATTGGTATTCTCAGGTCATC
ACAAAGTCAGAAATGATTGAATACCATGACATAAGTGGCTGTTATATTCTTCGTCCCTGG
GCCTATGCCATTTGGGAAGCCATCAAGGACTTTTTTGATGCTGAGATCAAGAAACTTGGT
GTTGAAAACTGCTACTTCCCCATGTTTGTGTCTCAAAGTGCATTAGAGAAAGAGAAGACT
CATGTTGCTGACTTTGCCCCAGAGGTTGCTTGGGTTACAAGATCTGGCAAAACCGAGCTG
GCAGAACCAATTGCCATTCGTCCTACTAGTGAAACAGTAATGTATCCTGCATATGCAAAA
TGGGTACAATCACACAGAGACCTGCCCATCAAGCTCAATCAGTGGTGCAATGTGGTGCGT
TGGGAATTCAAGCATCCTCAGCCTTTCCTACGTACTCGTGAATTTCTTTGGCAGGAAGGG
CACAGTGCTTTTGCTACCATGGAAGAGGCAGCGGAAGAGGTCTTGCAGATACTTGACTTA
TATGCTCAGGTATATGAAGAACTCCTGGCAATTCCTGTTGTTAAAGGAAGAAAGACGGAA
AAGGAAAAATTTGCAGGAGGAGACTATACAACTACAATAGAAGCATTTATATCTGCTAGT
GGAAGAGCTATCCAGGGAGGAACATCACATCATTTAGGGCAGAATTTTTCCAAAATGTTT
GAAATCGTTTTTGAAGATCCAAAGATACCAGGAGAGAAGCAATTTGCCTATCAAAACTCC
TGGGGCCTGACAACTCGAACTATTGGTGTTATGACCATGGTTCATGGGGACAACATGGGT
TTAGTATTACCACCCCGTGTAGCATGTGTTCAGGTGGTGATTATTCCTTGTGGCATTACC
AATGCACTTTCTGAAGAAGACAAAGAAGCGCTGATTGCAAAATGCAATGATTATCGAAGG
CGATTACTCAGTGTTAACATCCGCGTTAGAGCTGATTTACGAGATAATTATTCTCCAGGT
TGGAAATTCAATCACTGGGAGCTCAAGGGAGTTCCCATTAGACTTGAAGTTGGGCCACGT
GATATGAAGAGCTGTCAGTTTGTAGCCGTCAGACGAGATACTGGAGAAAAGCTGACAGTT
GCTGAAAATGAGGCAGAGACTAAACTTCAAGCTATTTTGGAAGACATCCAGGTCACCCTT
TTCACAAGGGCTTCTGAAGACCTTAAGACTCATATGGTTGTGGCTAATACAATGGAAGAC
TTTCAGAAGATACTAGATTCTGGAAAGATTGTTCAGATTCCATTCTGTGGGGAAATTGAC
TGTGAGGACTGGATCAAAAAGACCACTGCCAGGGATCAAGATCTTGAACCTGGTGCTCCA
TCCATGGGAGCTAAAAGCCTTTGCATCCCCTTCAAACCACTCTGTGAACTGCAGCCTGGA
GCCAAATGTGTCTGTGGCAAGAACCCTGCCAAGTACTACACCTTATTTGGTCGCAGCTAC
TGA

1. Fett R, Knippers R: The primary structure of human glutaminyl-tRNA synthetase. A highly conserved core, amino acid repeat regions, and homologies with translation elongation factors. J Biol Chem. 1991 Jan 25;266(3):1448-55. [PubMed ]
2. Thommes P, Fett R, Schray B, Kunze N, Knippers R: The core region of human glutaminyl-tRNA synthetase homologies with the Escherichia coli and yeast enzymes. Nucleic Acids Res. 1988 Jun 24;16(12):5391-406. [PubMed ]
3. Cerini C, Kerjan P, Astier M, Gratecos D, Mirande M, Semeriva M: A component of the multisynthetase complex is a multifunctional aminoacyl-tRNA synthetase. EMBO J. 1991 Dec;10(13):4267-77. [PubMed ]
4. Kaiser E, Eberhard D, Knippers R: Exons encoding the highly conserved part of human glutaminyl-tRNA synthetase. J Mol Evol. 1992 Jan;34(1):45-53. [PubMed ]
5. Jeong EJ, Hwang GS, Kim KH, Kim MJ, Kim S, Kim KS: Structural analysis of multifunctional peptide motifs in human bifunctional tRNA synthetase: identification of RNA-binding residues and functional implications for tandem repeats. Biochemistry. 2000 Dec 26;39(51):15775-82. [PubMed ]

1. Glutamine- dependent asparagine synthetase
2. Cell cycle control protein TS11

MCGIWALFGSDDCLSVQCLSAMKIAHRGPDAFRFENVNGYTNCCFGFHRLAVVDPLFGMQ
PIRVKKYPYLWLCYNGEIYNHKKMQQHFEFEYQTKVDGEIILHLYDKGGIEQTICMLDGV
FAFVLLDTANKKVFLGRDTYGVRPLFKAMTEDGFLAVCSEAKGLVTLKHSATPFLKVEPF
LPGHYEVLDLKPNGKVASVEMVKYHHCRDVPLHALYDNVEKLFPGFEIETVKNNLRILFN
NAVKKRLMTDRRIGCLLSGGLDSSLVAATLLKQLKEAQVQYPLQTFAIGMEDSPDLLAAR
KVADHIGSEHYEVLFNSEEGIQALDEVIFSLETYDITTVRASVGMYLISKYIRKNTDSVV
IFSGEGSDELTQGYIYFHKAPSPEKAEEESERLLRELYLFDVLRADRTTAAHGLELRVPF
LDHRFSSYYLSLPPEMRIPKNGIEKHLLRETFEDSNLIPKEILWRPKEAFSDGITSVKNS
WFKILQEYVEHQVDDAMMANAAQKFPFNTPKTKEGYYYRQVFERHYPGRADWLSHYWMPK
WINATDPSARTLTHYKSAVKA

• Nitrogen Metabolism (map00910 )

• ATP + L-aspartate + L-glutamine = AMP + diphosphate + L-asparagine + L-glutamate

• Asn_synthase (PF00733 )
• GATase_2 (PF00310 )

• None

• None

ATGTGTGGCATTTGGGCGCTGTTTGGCAGTGATGATTGCCTTTCTGTTCAGTGTCTGAGT
GCTATGAAGATTGCACACAGAGGTCCAGATGCATTCCGTTTTGAGAATGTCAATGGATAC
ACCAACTGCTGCTTTGGATTTCACCGGTTGGCGGTAGTTGACCCGCTGTTTGGAATGCAG
CCAATTCGAGTGAAGAAATATCCGTATTTGTGGCTCTGTTACAATGGTGAAATCTACAAC
CATAAGAAGATGCAACAGCATTTTGAATTTGAATACCAGACCAAAGTGGATGGTGAGATA
ATCCTTCATCTTTATGACAAAGGAGGAATTGAGCAAACAATTTGTATGTTGGATGGTGTG
TTTGCATTTGTTTTACTGGATACTGCCAATAAGAAAGTGTTCCTGGGTAGAGATACATAT
GGAGTCAGACCTTTGTTTAAAGCAATGACAGAAGATGGATTTTTGGCTGTATGTTCAGAA
GCTAAAGGTCTTGTTACATTGAAGCACTCCGCGACTCCCTTTTTAAAAGTGGAGCCTTTT
CTTCCTGGACACTATGAAGTTTTGGATTTAAAGCCAAATGGCAAAGTTGCATCCGTGGAA
ATGGTTAAATATCATCACTGTCGGGATGTACCCCTGCACGCCCTCTATGACAATGTGGAG
AAACTCTTTCCAGGTTTTGAGATAGAAACTGTGAAGAACAACCTCAGGATCCTTTTTAAT
AATGCTGTAAAGAAACGTTTGATGACAGACAGAAGGATTGGCTGCCTTTTATCAGGGGGC
TTGGACTCCAGCTTGGTTGCTGCCACTCTGTTGAAGCAGCTGAAAGAAGCCCAAGTACAG
TATCCTCTCCAGACATTTGCAATTGGCATGGAAGACAGCCCCGATTTACTGGCTGCTAGA
AAGGTGGCAGATCATATTGGAAGTGAACATTATGAAGTCCTTTTTAACTCTGAGGAAGGC
ATTCAGGCTCTGGATGAAGTCATATTTTCCTTGGAAACTTATGACATTACAACAGTTCGT
GCTTCAGTAGGTATGTATTTAATTTCCAAGTATATTCGGAAGAACACAGATAGCGTGGTG
ATCTTCTCTGGAGAAGGATCAGATGAACTTACGCAGGGTTACATATATTTTCACAAGGCT
CCTTCTCCTGAAAAAGCCGAGGAGGAGAGTGAGAGGCTTCTGAGGGAACTCTATTTGTTT
GATGTTCTCCGCGCAGATCGAACTACTGCTGCCCATGGTCTTGAACTGAGAGTCCCATTT
CTAGATCATCGATTTTTTTCCTATTACTTGTCTCTGCCACCAGAAATGAGAATTCCAAAG
AATGGGATAGAAAAACATCTCCTGAGAGAGACGTTTGAGGATTCCAATCTGATACCCAAA
GAGATTCTCTGGCGACCAAAAGAAGCCTTCAGTGATGGAATAACTTCAGTTAAGAATTCC
TGGTTTAAGATTTTACAGGAATACGTTGAACATCAGGTTGATGATGCAATGATGGCAAAT
GCAGCCCAGAAATTTCCCTTCAATACTCCTAAAACCAAAGAAGGATATTACTACCGTCAA
GTCTTTGAACGCCATTACCCAGGCCGGGCTGACTGGCTGAGCCATTACTGGATGCCCAAG
TGGATCAATGCCACTGACCCTTCTGCCCGCACGCTGACCCACTACAAGTCAGCTGTCAAA
GCTTAG

1. Andrulis IL, Chen J, Ray PN: Isolation of human cDNAs for asparagine synthetase and expression in Jensen rat sarcoma cells. Mol Cell Biol. 1987 Jul;7(7):2435-43. [PubMed ]
2. Zhang YP, Lambert MA, Cairney AE, Wills D, Ray PN, Andrulis IL: Molecular structure of the human asparagine synthetase gene. Genomics. 1989 Apr;4(3):259-65. [PubMed ]
3. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed ]
4. Greco A, Ittmann M, Basilico C: Molecular cloning of a gene that is necessary for G1 progression in mammalian cells. Proc Natl Acad Sci U S A. 1987 Mar;84(6):1565-9. [PubMed ]
5. Greco A, Gong SS, Ittmann M, Basilico C: Organization and expression of the cell cycle gene, ts11, that encodes asparagine synthetase. Mol Cell Biol. 1989 Jun;9(6):2350-9. [PubMed ]
6. Van Heeke G, Schuster SM: Expression of human asparagine synthetase in Escherichia coli. J Biol Chem. 1989 Apr 5;264(10):5503-9. [PubMed ]
7. Van Heeke G, Schuster SM: The N-terminal cysteine of human asparagine synthetase is essential for glutamine-dependent activity. J Biol Chem. 1989 Nov 25;264(33):19475-7. [PubMed ]

1. GDH

MYRYLAKALLPSRAGPAALGSAANHSAALLGRGRGQPAAASQPGLALAARRHYSELVADR
EDDPNFFKMVEGFFDRGASIVEDKLVKDLRTQESEEQKRNRVRGILRIIKPCNHVLSLSF
PIRRDDGSWEVIEGYRAQHSQHRTPCKGGIRYSTDVSVDEVKALASLMTYKCAVVDVPFG
GAKAGVKINPKNYTENELEKITRRFTMELAKKGFIGPGVDVPAPDMNTGEREMSWIADTY
ASTIGHYDINAHACVTGKPISQGGIHGRISATGRGVFHGIENFINEASYMSILGMTPGFR
DKTFVVQGFGNVGLHSMRYLHRFGAKCIAVGESDGSIWNPDGIDPKELEDFKLQHGSILG
FPKAKPYEGSILEVDCDILIPAATEKQLTKSNAPRVKAKIIAEGANGPTTPEADKIFLER
NILVIPDLYLNAGGVTVSYFEWLKNLNHVSYGRLTFKYERDSNYHLLLSVQESLERKFGK
HGGTIPIVPTAEFQDSISGASEKDIVHSALAYTMERSARQIMHTAMKYNLGLDLRTAAYV
NAIEKVFKVYSEAGVTFT

• Arginine and Proline Metabolism (map00330 )
• D-Glutamine and D-Glutamate Metabolism (map00471 )
• Glutamate Metabolism (map00251 )
• Nitrogen Metabolism (map00910 )

• L-glutamate + H2O + NAD(P)+ = 2-oxoglutarate + ammonia + NAD(P)H + H+

• ELFV_dehydrog (PF00208 )
• ELFV_dehydrog_N (PF02812 )

• None

• None

ATGTACCGCTACCTGGCCAAAGCGCTGCTGCCGTCCCGGGCCGGGCCCGCTGCCCTGGGC
TCCGCGGCCAACCACTCGGCCGCGTTGCTGGGCCGGGGCCGCGGACAGCCCGCCGCCGCC
TCGCAGCCGGGGCTCGCATTGGCCGCCCGGCGCCACTACAGCGAGTTGGTGGCCGACCGC
GAGGACGACCCCAACTTCTTCAAGATGGTGGAGGGCTTCTTCGATCGCGGCGCCAGCATC
GTGGAGGACAAGTTGGTGAAGGACCTGAGGACCCAGGAAAGCGAGGAGCAGAAGCGGAAC
CGGGTGCGCGGCATCCTGCGGATCATCAAGCCCTGCAACCATGTGCTGAGTCTCTCCTTC
CCCATCCGGCGCGACGACGGCTCCTGGGAGGTCATCGAAGGCTACCGGGCCCAGCACAGC
CAGCACCGCACGCCCTGCAAGGGAGGTATCCGTTACAGCACTGATGTGAGTGTAGATGAA
GTAAAAGCTTTGGCTTCTCTGATGACATACAAGTGTGCAGTGGTTGATGTGCCGTTTGGG
GGTGCTAAAGCTGGTGTTAAGATCAATCCCAAGAACTATACCGAAAATGAATTGGAAAAG
ATCACAAGGAGGTTCACCATGGAGCTAGCAAAGAAGGGCTTTATTGGTCCTGGCGTTGAT
GTGCCTGCTCCAGACATGAACACAGGTGAGCGGGAGATGTCCTGGATTGCTGATACCTAT
GCCAGCACCATAGGGCACTATGATATTAATGCACACGCCTGTGTTACTGGTAAACCCATC
AGCCAAGGGGGAATCCATGGACGCATCTCTGCTACTGGCCGTGGTGTCTTCCATGGGATT
GAAAACTTCATCAATCAAGCTTCTTACATGAGCATTTTAGGAATGACACCAGGGTTTAGA
GATAAAACATTTGTTGTTCAGGGATTTGGTAATGTGGGCCTACACTCTATGAGATATTTA
CATCGTTTTGGTGCTAAATGTATTGCTGTTGGTGAGTCTGATGGGAGTATATGGAATCCA
GATGGTATTGACCCAAAGGAACTGGAAGACTTCAAATTGCAACATGGGTCCATTCTGGGC
TTCCCCAAGGCAAAGCCCTATGAAGGAAGCATCTTGGAGGTCGACTGTGACATACTGATC
CCAGCTGCCACTGAGAAGCAGTTGACCAAATCCAACGCACCCAGAGTCAAAGCCAAGATC
ATTGCTGAAGGTGCCAATGGGCCAACAACTCCAGAAGCTGATAAGATCTTCCTGGAGAGA
AACATTTTGGTTATTCCAGATCTCTACTTGAATGCTGGAGGAGTGACAGTATCTTACTTT
GAGTGGCTGAAGAATCTAAATCATGTCAGCTATGGCCGTTTGACCTTCAAATATGAAAGG
GATTCTAACTACCACTTGCTCCTGTCTGTTCAAGAGAGTTTAGAAAGAAAATTTGGAAAG
CATGGTGGAACTATTCCCATTGTACCCACGGCAGAGTTCCAAGACAGTATATCGGGTGCA
TCTGAGAAAGACATTGTGCACTCTGCCTTGGCATACACAATGGAGCGTTCTGCCAGGCAA
ATTATGCACACAGCCATGAAGTATAACCTGGGATTGGACCTGAGAACAGCTGCCTATGTC
AATGCCATTGAAAAAGTCTTCAAAGTGTACAGTGAAGCTGGTGTGACCTTCACATAG

1. Shashidharan P, Michaelidis TM, Robakis NK, Kresovali A, Papamatheakis J, Plaitakis A: Novel human glutamate dehydrogenase expressed in neural and testicular tissues and encoded by an X-linked intronless gene. J Biol Chem. 1994 Jun 17;269(24):16971-6. [PubMed ]

1. Glutamate--ammonia ligase
2. GS

MTTSASSHLNKGIKQVYMSLPQGEKVQAMYIWIDGTGEGLRCKTRTLDSEPKCVEELPEW
NFDGSSTLQSEGSNSDMYLVPAAMFRDPFRKDPNKLVLCEVFKYNRRPAETNLRHTCKRI
MDMVSNQHPWFGMEQEYTLMGTDGHPFGWPSNGFPGPQGPYYCGVGADRAYGRDIVEAHY
RACLYAGVKIAGTNAEVMPAQWEFQIGPCEGISMGDHLWVARFILHRVCEDFGVIATFDP
KPIPGNWNGAGCHTNFSTKAMREENGLKYIEEAIEKLSKRHQYHIRAYDPKGGLDNARRL
TGFHETSNINDFSAGVANRSASIRIPRTVGQEKKGYFEDRRPSANCDPFSVTEALIRTCL
LNETGDEPFQYKN

• Glutamate Metabolism (map00251 )
• Nitrogen Metabolism (map00910 )
• Peptidoglycan biosynthesis (map00550 )

• ATP + L-glutamate + ammonia = ADP + phosphate + L-glutamine

• Gln-synt_C (PF00120 )
• Gln-synt_N (PF03951 )

• None

• None

ATGACCACCTCAGCAAGTTCCCACTTAAATAAAGGCATCAAGCAGGTGTACATGTCCCTG
CCTCAGGGTGAGAAAGTCCAGGCCATGTATATCTGGATCGATGGTACTGGAGAAGGACTG
CGCTGCAAGACCCGGACCCTGGACAGTGAGCCCAAGTGTGTGGAAGAGTTGCCTGAGTGG
AATTTCGATGGCTCCAGTACTTTACAGTCTGAGGGTTCCAACAGTGACATGTATCTCGTG
CCTGCTGCCATGTTTCGGGACCCCTTCCGTAAGGACCCTAACAAGCTGGTGTTATGTGAA
GTTTTCAAGTACAATCGAAGGCCTGCAGAGACCAATTTGAGGCACACCTGTAAACGGATA
ATGGACATGGTGAGCAACCAGCACCCCTGGTTTGGCATGGAGCAGGAGTATACCCTCATG
GGGACAGATGGGCACCCCTTTGGTTGGCCTTCCAACGGCTTCCCAGGGCCCCAGGGTCCA
TATTACTGTGGTGTGGGAGCAGACAGAGCCTATGGCAGGGACATCGTGGAGGCCCATTAC
CGGGCCTGCTTGTATGCTGGAGTCAAGATTGCGGGGACTAATGCCGAGGTCATGCCTGCC
CAGTGGGAATTTCAGATTGGACCTTGTGAAGGAATCAGCATGGGAGATCATCTCTGGGTG
GCCCGTTTCATCTTGCATCGTGTGTGTGAAGACTTTGGAGTGATAGCAACCTTTGATCCT
AAGCCCATTCCTGGGAACTGGAATGGTGCAGGCTGCCATACCAACTTCAGCACCAAGGCC
ATGCGGGAGGAGAATGGTCTGAAGTACATCGAGGAGGCCATTGAGAAACTAAGCAAGCGG
CACCAGTACCACATCCGTGCCTATGATCCCAAGGGAGGCCTGGACAATGCCCGACGTCTA
ACTGGATTCCATGAAACCTCCAACATCAACGACTTTTCTGGTGGTGTAGCCAATCGTAGC
GCCAGCATACGCATTCCCCGGACTGTTGGCCAGGAGAAGAAGGGTTACTTTGAAGATCGT
CGCCCCTCTGCCAACTGCGACCCCTTTTCGGTGACAGAAGCCCTCATCCGCACGTGTCTT
CTCAATGAAACCGGCGATGAGCCCTTCCAGTACAAAAATTAA

1. Gibbs CS, Campbell KE, Wilson RH: Sequence of a human glutamine synthetase cDNA. Nucleic Acids Res. 1987 Aug 11;15(15):6293. [PubMed ]
2. Van den Hoff MJ, Geerts WJ, Das AT, Moorman AF, Lamers WH: cDNA sequence of the long mRNA for human glutamine synthase. Biochim Biophys Acta. 1991 Oct 8;1090(2):249-51. [PubMed ]
3. Christa L, Simon MT, Flinois JP, Gebhardt R, Brechot C, Lasserre C: Overexpression of glutamine synthetase in human primary liver cancer. Gastroenterology. 1994 May;106(5):1312-20. [PubMed ]
4. Boksha IS, Schonfeld HJ, Langen H, Muller F, Tereshkina EB, Burbaeva GSh: Glutamine synthetase isolated from human brain: octameric structure and homology of partial primary structure with human liver glutamine synthetase. Biochemistry (Mosc). 2002 Sep;67(9):1012-20. [PubMed ]

1. UTP--ammonia ligase 1
2. CTP synthetase 1

MKYILVTGGVISGIGKGIIASSVGTILKSCGLHVTSIKIDPYINIDAGTFSPYEHGEVFV
LDDGGEVDLDLGNYERFLDIRLTKDNNLTTGKIYQYVINKERKGDYLGKTVQVVPHITDA
IQEWVMRQALIPVDEDGLEPQVCVIELGGTVGDIESMPFIEAFRQFQFKVKRENFCNIHV
SLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHVEPEQ
VICVHDVSSIYRVPLLLEEQGVVDYFLRRLDLPIERQPRKMLMKWKEMADRYDRLLETCS
IALVGKYTKFSDSYASVIKALEHSALAINHKLEIKYIDSADLEPITSQEEPVRYHEAWQK
LCSAHGVLVPGGFGVRGTEGKIQAIAWARNQKKPFLGVCLGMQLAVVEFSRNVLGWQDAN
STEFDPTTSHPVVVDMPEHNPGQMGGTMRLGKRRTLFQTKNSVMRKLYGDADYLEERHRH
RFEVNPVWKKCLEEQGLKFVGQDVEGERMEIVELEDHPFFVGVQYHPEFLSRPIKPSPPY
FGLLLASVGRLSHYLQKGCRLSPRDTYSDRSGSSSPDSEITELKFPSINHD

• Pyrimidine Metabolism (map00240 )

• ATP + UTP + NH3 = ADP + phosphate + CTP

• CTP_synth_N (PF06418 )
• GATase (PF00117 )

• None

• None

ATGAAGTACATTCTGGTTACTGGTGGTGTTATATCAGGAATTGGAAAAGGAATCATTGCC
AGCAGTGTGGGCACAATACTCAAGTCATGTGGTTTACATGTAACTTCAATCAAAATTGAC
CCCTACATTAACATTGATGCAGGAACATTCTCTCCTTATGAGCATGGTGAGGTTTTTGTG
CTGGATGATGGTGGGGAAGTAGACCTTGACCTGGGTAACTATGAGCGGTTCCTTGACATC
CGCCTCACCAAGGACAATAATCTGACCACTGGAAAGATATACCAGTATGTCATTAACAAG
GAACGGAAAGGAGATTACTTGGGGAAAACTGTCCAAGTTGTCCCTCATATCACAGATGCA
ATCCAGGAGTGGGTGATGAGACAGGCGTTAATACCTGTAGATGAAGATGGCCTGGAACCT
CAAGTGTGTGTTATTGAGCTTGGTGGAACCGTGGGGGACATAGAAAGCATGCCCTTTATT
GAGGCCTTCCGTCAGTTCCAATTCAAGGTCAAAAGAGAGAACTTTTGTAACATCCACGTC
AGTCTAGTTCCCCAGCCAAGTTCAACAGGGGAACAGAAGACTAAACCTACCCAGAATAGT
GTTCGGGAACTTAGAGGACTTGGGCTTTCCCCAGATCTGGTTGTATGCAGGTGCTCAAAT
CCACTTGACACATCAGTGAAGGAGAAAATATCAATGTTCTGCCATGTTGAGCCTGAACAA
GTGATCTGTGTCCACGATGTCTCATCCATCTACCGAGTCCCCTTGTTGTTAGAGGAGCAA
GGGGTTGTAGATTATTTTCTTCGAAGACTTGACCTTCCTATTGAGAGGCAGCCAAGAAAA
ATGCTGATGAAATGGAAAGAGATGGCTGACAGATATGATCGCTTGCTGGAGACCTGCTCT
ATTGCCCTTGTGGCGAAATACACCGAGTTCTCAGACTCCTATGCCTCTGTCATTAAGGCT
CTGGAGCATTCTGCACTGGCCATCAACCACAAATTGGAAATCAAGTACATAGATTCTGCG
GACTTGGAGCCCATCACCTCGCAAGAAGAGCCCGTGCGCTACCACGAAGCTTGGCAGAAG
CTCTGTAGTGCTCATGGAGTGCTGGTTCCAGGAGGATTTGGTGTTCGAGGAACAGAAGGA
AAAATCCAAGCAATTGCCTGGGCTCGGAATCAGAAAAAGCCTTTTTTGGGCGTGTGCTTA
GGGATGCAGTTGGCAGTGGTTGAATTCTCAAGAAACGTGCTGGGATGGCAAGATGCCAAT
TCTACAGAGTTTGACCCTACGACCAGTCATCCCGTGGTCGTAGACATGCCAGAACACAAC
CCAGGGCAGATGGGCGGAACCATGAGGCTGGGCAAGAGGAGAACCCTGTTCCAGACCAAG
AACTCAGTCATGAGGAAACTCTATGGAGACGCAGACTACTTGGAAGAGAGGCACCGCCAC
CGATTTGAGGTGAATCCAGTCTGGAAAAAGTGTTTGGAAGAACAAGGCTTGAAGTTTGTT
GGCCAAGATGTTGAAGGAGAGAGAATGGAAATTGTGGAGTTAGAAGATCATCCCTTTTTT
GTTGGGGTTCAGTACCACCCTGAGTTCCTGTCCAGGCCTATCAAGCCCTCCCCACCATAC
TTTGGCCTCCTCCTGGCCTCTGTGGGGCGGCTCTCACATTACCTCCAGAAAGGCTGCAGG
CTCTCACCCAGGGACACCTATAGTGACAGGAGTGGAAGCAGCTCCCCTGACTCTGAAATC
ACCGAACTGAAGTTTCCATCAATAAATCATGACTGA

1. Yamauchi M, Yamauchi N, Meuth M: Molecular cloning of the human CTP synthetase gene by functional complementation with purified human metaphase chromosomes. EMBO J. 1990 Jul;9(7):2095-9. [PubMed ]

1. GLS
2. L-glutamine amidohydrolase
3. K-glutaminase

MMRLRGSGMLRDLLLRSPAGVSATLRRAQPLVTLCRRPRGGGRPAAGPAAAARLHPWWGG
GGWPAEPLARGLSSSPSEILQELGKGSTHPQPGVSPPAAPAAPGPKDGPGETDAFGNSEG
KELVASGENKIKQGLLPSLEDLLFYTIAEGQEKIPVHKFITALKSTGLRTSDPRLKECMD
MLRLTLQTTSDGVMLDKDLFKKCVQSNIVLLTQAFRRKFVIPDFMSFTSHIDELYESAKK
QSGGKVADYIPQLAKFSPDLWGVSVCTVDGQRHSTGDTKVPFCLQSCVKPLKYAIAVNDL
GTEYVHRYVGKEPSGLRFNKLFLNEDDKPHNPMVNAGAIVVTSLIKQGVNNAEKFDYVMQ
FLNKMAGNEYVGFSNATFQSERESGDRNFAIGYYLKEKKCFPEGTDMVGILDFYFQLCSI
EVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYDFSGQFAFHVGLPA
KSGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKGIHFCHDLVSLCNFHNYDNLRHFAKKL
DPRREGGDQRVKSVINLLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVE
VVKFLLEACKVNPFPKDRWNNTPMDEALHFGHHDVFKILQEYQVQYTPQGDSDNGKENQT
VHKNLDGLL

• D-Glutamine and D-Glutamate Metabolism (map00471 )
• Glutamate Metabolism (map00251 )
• Nitrogen Metabolism (map00910 )

• L-glutamine + H2O = L-glutamate + NH3

• Ank (PF00023 )
• Glutaminase (PF04960 )

• 1-23

ATGATGCGGCTGCGAGGCTCGGGGATGCTGCGGGACCTGCTCCTGCGGTCGCCCGCCGGC
GTGAGCGNGACTCTGCGGCGGGCACAGCCCTTGGTCACCCTGTGCCGGCGTCCCCGAGGC
GGGGGACGGCCGGCCGCGGGCCCGGCTGCCGCCGCGCGACTCCACCCGTGGTGGGGCGGG
GGCGGCTGGCCGGCGGAGCCCCTCGCGCGGGGCCTGTCCAGCTCTCCTTCGGAGATCTTG
CAGGAGCTGGGCAAGGGGAGCACGCATCCCCAGCCCGGGGTGTCGCCACCCGCTGCCCCG
GCGGCGCCCGGCCCCAAGGACGGCCCCGGGGAGACGGACGCGTTTGGCAACAGCGAGGGC
AAAGAGCTGGTGGCCTCAGGTGAAAACAAAATAAAACAGGGTCTGTTACCTAGCTTGGAA
GATTTGCTGTTCTATACAATTGCTGAAGGACAAGAGAAAATACCTGTTCATAAATTTATT
ACAGCACTCAAATCTACAGGATTGCGAACGTCTGATCCCAGGTTGAAAGAGTGTATGGAT
ATGTTAAGATTAACTCTTCAAACAACATCAGATGGTGTCATGCTAGACAAAGATCTTTTT
AAAAAATGTGTTCAGAGCAACATTGTTTTGTTGACACAAGCATTTAGAAGAAAGTTTGTG
ATTCCTGACTTTATGTCTTTTACCTCACACATTGATGAGTTATATGAAAGTGCTAAAAAG
CAGTCTGGAGGAAAGGTTGCAGATTATATTCCTCAACTGGCCAAATTCAGTCCCGATTTG
TGGGGTGTGTCTGTTTGTACAGCAGATGGACAGAGGCATTCTACTGGAGATACCAAAGTT
CCCTTCTGTCTTCAGTCCTGTGTAAAACCTTTGAAATATGCCATTGCTGTTAATGATCTT
GGAACTGAATATGTGCATCGATATGTTGGAAAAGAGCCGAGTGGACTAAGATTCAACAAA
CTATTTTTGAATGAAGATGATAAACCACATAATCCTATGGTAAATGCTGGAGCAATTGTT
GTGACTTCACTAATAAAGCAAGGAGTAAATAATGCTGAAAAATTTGACTATGTCATGCAG
TTTTTGAATAAGATGGCTGGTAATGAATATGTTGGATTCAGTAATGCAACGTTTCAGTCT
GAAAGAGAAAGTGGAGATCGAAATTTTGCAATAGGATATTACTTAAAAGAAAAGAAGTGT
TTTCCAGAAGGCACAGACATGGTTGGTATATTAGACTTCTACTTCCAGCTGTGCTCCATT
GAAGTGACTTGTGAATCAGCCAGTGTGATGGCTGCGACACTGGCTAATGGTGGTTTCTGC
CCAATTACTGGTGAAAGAGTACTGAGCCCTGAAGCAGTTCGAAATACATTGAGTTTGATG
CATTCCTGTGGCATGTATGACTTCTCAGGGCAGTTTGCTTTCCATGTTGGTCTTCCTGCA
AAATCTGGAGTTGCTGGGGGCATTCTTTTAGTTGTCCCCAATGTTATGGGTATGATGTGC
TGGTCTCCTCCTCTGGATAAGATGGGCAACAGTGTTAAGGGAATTCACTTTTGTCACGAT
CTTGTTTCTCTGTGTAATTTCCATAACTATGATAATTTGAGACACTTTGCAAAAAAACTT
GATCCTCGAAGAGAAGGTGGTGATCAAAGGCATTCCTTTGGACCATTGGACTATGAAAGT
CTCCAACAAGAACTTGCTTTAAAAGAGACAGTATGGAAAAAAGTGTCACCTGAGTCAAAT
GAGGACATCTCTACAACTGTAGTATATAGAATGGAAAGTCTGGGAGAGAAAAGCTAA

1. Elgadi KM, Meguid RA, Qian M, Souba WW, Abcouwer SF: Cloning and analysis of unique human glutaminase isoforms generated by tissue-specific alternative splicing. Physiol Genomics. 1999 Aug 31;1(2):51-62. [PubMed ]
2. Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1998 Dec 31;5(6):355-64. [PubMed ]
3. Holcomb T, Taylor L, Trohkimoinen J, Curthoys NP: Isolation, characterization and expression of a human brain mitochondrial glutaminase cDNA. Brain Res Mol Brain Res. 2000 Mar 10;76(1):56-63. [PubMed ]

1. Formiminotransferase- cyclodeaminase
2. FTCD
3. LCHC1[Includes: Glutamate formimidoyltransferase
4. Glutamate formiminotransferase
5. Glutamate formyltransferase
6. Formimidoyltetrahydrofolate cyclodeaminase
7. Formiminotetrahydrofolate cyclodeaminase]

MSQLVECVPNFSEGKNQEVIDAISGAITQTPGCVLLDVDAGPSTNRTVYTFVGPPECVVE
GALNAARVASRLIDMSRHQGEHPRMGALDVCPFIPVRGVSVDECVLCAQAFGQRLAEELD
VPVYLYGEAARMDSRRTLPAIRAGEYEALPKKLQQADWAPDFGPSSFVPSWGATATGARK
FLIAFNINLLGTKEQAHRIALNLREQGRGKDQPGRLKKVQGIGWYLDEKNLAQVSTNLLD
FEVTALHTVYEETCREAQELSLPVVGSQLVGLVPLKALLDAAAFYCEKENLFILEEEQRI
RLVVSRLGLDSLCPFSPKERIIEYLVPERGPERGLGSKSLRAFVGEVGARSAAPGGGSVA
AAAAAMGAALGSMVGLMTYGRRQFQSLDTTMRRLIPPFREASAKLTTLVDADAEAFTAYL
EAMRLPKNTPEEKDRRTAALQEGLRRAVSVPLTLAETVASLWPALQELARCGNLACRSDL
QVAAKALEMGVFGAYFNVLINLRDITDEAFKDQIHHRVSSLLQEAKTQAALVLDCLETRQ
E

• One Carbon Pool By Folate (map00670 )

• 5-formimidoyltetrahydrofolate = 5,10-methenyltetrahydrofolate + NH3

• FTCD (PF02971 )
• FTCD_C (PF04961 )
• FTCD_N (PF07837 )

• None

• None

ATGTCCCAGCTGGTGGAATGCGTCCCCAACTTTTCGGAGGGGAAGAACCAGGAGGTGATC
GACGCCATCTCTGGAGCCATCACACAGACCCCGGGCTGCGTGCTGCTGGATGTGGACGCA
GGCCCTTCCACCAACCGCACCGTGTACACCTTCGTGGGGCCGCCGGAGTGCGTGGTGGAG
GGGGCCCTCAACGCTGCCCGGGTAGCTTCCCGACTTATCGACATGAGCAGGCACCAAGGA
GAGCACCCCCGCATGGGGGCCCTAGACGTCTGCCCCTTCATCCCCGTGAGGGGCGTCAGC
GTGGATGAGTGTGTGCTCTGCGCCCAGGCCTTTGGCCAGAGGCTGGCAGAGGAGCTGGAC
GTGCCAGTTTACCTGTACGGCGAGGCAGCCAGGATGGACAGTCGCCGGACCCTGCCGGCC
ATCCGGGCCGGGGAGTACGAGGCCCTCCCTAAGAAGCTCCAGCAGGCCGACTGGGCGCCC
GACTTTGGTCCCAGCTCCTTTGTCCCCAGTTGGGGGGCCACGGCCACGGGGGCGAGGAAG
TTCCTCATTGCTTTTAACATCAACCTGCTCGGCACAAAGGAGCAAGCCCACCGCATCGCG
CTCAACCTGCGGGAGCAGGGCCGCGGGAAGGACCAGCCAGGACGTCTGAAGAAAGTTCAG
GGCATTGGCTGGTACCTGGATGAGAAGAACCTGGCTCAGGTGTCCACCAATCTTCTGGAC
TTTGAGGTCACGGCACTGCACACGGTCTACGAGGAGACCTGCCGAGAAGCACAGGAGCTG
AGCCTCCCAGTGGTGGGCTCACAGCTGGTGGGCCTGGTGCCCCTGAAGGCTCTGCTGGAT
GCGGCCGCCTTCTACTGCGAGAAGGAGAACCTCTTCATCCTGGAGGAGGAGCAGCGGATC
AGGCTGGTGGTGAGCCGGCTGGGCCTGGACTCCCTGTGCCCCTTCAGCCCTAAGGAGCGG
ATCATCGAGTACCTGGTCCCTGAGCGCGGGCCTGAGCGAGGCCTGGGCAGCAAGTCCCTG
CGCGCCTTCGTGGGGGAGGTGGGTGCCCGCTCTGCGGCCCCCGGGGGCGGCTCGGTGGCG
GCGGCCGCTGCGGCCATGGGTGCGGCGCTGGGCTCCATGGTGGGCCTCATGACCTACGGG
CGGCGCCAATTCCAGTCCCTGGACACGACGATGCGGCGCCTGATCCCGCCCTTCCGCGAG
GCTTCGGCCAAGCTAACCACGCTGGTGGATGCCGACGCCGAGGCCTTCACCGCCTACCTG
GAAGCAATGAGGCTCCCCAAGAACACACCTGAGGAAAAGGACAGGCGCACGGCGGCCCTA
CAGGAGGGTCTGAGGCGGGCAGTCTCTGTGCCGCTGACGCTGGCGGAGACGGTGGCCTCG
CTGTGGCCGGCGCTGCAGGAACTGGCCCGGTGTGGGAACCTGGCCTGCCGGTCAGACCTC
CAGGTGGCGGCCAAAGCCCTGGAGATGGGCGTGTTTGGCGCATATTTCAACGTGCTCATC
AACCTGAGGGACATCACAGACGAGGCATTTAAGGACCAGATCCACCATCGTGTTTCCAGC
CTCCTGCAGGAAGCCAAGACCCAGGCTGCACTGGTGCTGGACTGCTTGGAGACCCGGCAG
GAGTGA

1. Solans A, Estivill X, de la Luna S: Cloning and characterization of human FTCD on 21q22.3, a candidate gene for glutamate formiminotransferase deficiency. Cytogenet Cell Genet. 2000;88(1-2):43-9. [PubMed ]
2. Lapierre P, Hajoui O, Homberg JC, Alvarez F: Formiminotransferase cyclodeaminase is an organ-specific autoantigen recognized by sera of patients with autoimmune hepatitis. Gastroenterology. 1999 Mar;116(3):643-9. [PubMed ]
3. Hilton JF, Christensen KE, Watkins D, Raby BA, Renaud Y, de la Luna S, Estivill X, MacKenzie RE, Hudson TJ, Rosenblatt DS: The molecular basis of glutamate formiminotransferase deficiency. Hum Mutat. 2003 Jul;22(1):67-73. [PubMed ]

1. GDH

MYRYLGEALLLSRAGPAALGSASADSAALLGWARGQPAAAPQPGLALAARRHYSEAVADR
EDDPNFFKMVEGFFDRGASIVEDKLVEDLRTRESEEQKRNRVRGILRIIKPCNHVLSLSF
PIRRDDGSWEVIEGYRAQHSQHRTPCKGGIRYSTDVSVDEVKALASLMTYKCAVVDVPFG
GAKAGVKINPKNYTDNELEKITRRFTMELAKKGFIGPGIDVPAPDMSTGEREMSWIADTY
ASTIGHYDINAHACVTGKPISQGGIHGRISATGRGVFHGIENFINEASYMSILGMTPGFG
DKTFVVQGFGNVGLHSMRYLHRFGAKCIAVGESDGSIWNPDGIDPKELEDFKLQHGSILG
FPKAKPYEGSILEADCDILIPAASEKQLTKSNAPRVKAKIIAEGANGPTTPEADKIFLER
NIMVIPDLYLNAGGVTVSYFEWLKNLNHVSYGRLTFKYERDSNYHLLMSVQESLERKFGK
HGGTIPIVPTAEFQDRISGASEKDIVHSGLAYTMERSARQIMRTAMKYNLGLDLRTAAYV
NAIEKVFKVYNEAGVTFT

• Arginine and Proline Metabolism (map00330 )
• D-Glutamine and D-Glutamate Metabolism (map00471 )
• Glutamate Metabolism (map00251 )
• Nitrogen Metabolism (map00910 )

• L-glutamate + H2O + NAD(P)+ = 2-oxoglutarate + ammonia + NAD(P)H + H+

• ELFV_dehydrog (PF00208 )
• ELFV_dehydrog_N (PF02812 )

• 1-20

ATGTACCGCTACCTGGGCGAAGCGCTGTTGCTGTCCCGGGCCGGGCCCGCTGCCCTGGGC
TCGGCGTCCGCCGACTCGGCCGCGTTGCTGGGCTGGGCCCGGGGACAGCCCGCCGCCGCC
CCGCAGCCGGGGCTGGCATTGGCCGCCCGGCGCCACTACAGCGAGGCGGTGGCCGACCGC
GAGGACGACCCCAACTTCTTCAAGATGGTGGAGGGCTTCTTCGATCGCGGCGCCAGCATC
GTGGAGGACAAGCTGGTGGAGGACCTGAGGACCCGGGAGAGCGAGGAGCAGAAGCGGAAC
CGGGTGCGCGGCATCCTGCGGATCATCAAGCCCTGCAACCATGTGCTGAGTCTCTCCTTC
CCCATCCGGCGCGACGACGGCTCCTGGGAGGTCATCGAAGGCTACCGGGCCCAGCACAGC
CAGCACCGCACGCCCTGCAAGGGAGGTATCCGTTACAGCACTGATGTGAGTGTAGATGAA
GTAAAAGCTTTGGCTTCTCTGATGACATACAAGTGTGCAGTGGTTGATGTGCCGTTTGGG
GGTGCTAAAGCTGGTGTTAAGATCAATCCCAAGAACTATACTGATAATGAATTGGAAAAG
ATCACAAGGAGGTTCACCATGGAGCTAGCAAAAAAGGGCTTTATTGGTCCTGGCATTGAT
GTGCCTGCTCCAGACATGAGCACAGGTGAGCGGGAGATGTCCTGGATCGCTGATACCTAT
GCCAGCACCATAGGGCACTATGATATTAATGCACACGCCTGTGTTACTGGTAAACCCATC
AGCCAAGGGGGAATCCATGGACGCATCTCTGCTACTGGCCGTGGTGTCTTCCATGGGATT
GAAAATTTCATCAATGAAGCTTCTTACATGAGCATTTTAGGAATGACACCAGGGTTTGGA
GATAAAACATTTGTTGTTCAGGGATTTGGTAATGTGGGCCTACACTCTATGAGATATTTA
CATCGTTTTGGTGCTAAATGTATTGCTGTTGGTGAGTCTGATGGGAGTATATGGAATCCA
GATGGTATTGACCCAAAGGAACTGGAAGACTTCAAATTGCAACATGGGTCCATTCTGGGC
TTCCCCAAGGCAAAGCCCTATGAAGGAAGCATCTTGGAGGCCGACTGTGACATACTGATC
CCAGCTGCCAGTGAGAAGCAGTTGACCAAATCCAACGCACCCAGAGTCAAAGCCAAGATC
ATTGCTGAAGGTGCCAATGGGCCAACAACTCCAGAAGCTGACAAGATCTTCCTGGAGAGA
AACATTATGGTTATTCCAGATCTCTACTTGAATGCTGGAGGAGTGACAGTATCTTACTTT
GAGTGGCTGAAGAATCTAAATCATGTCAGCTATGGCCGTTTGACCTTCAAATATGAAAGG
GATTCTAACTACCACTTGCTCATGTCTGTTCAAGAGAGTTTAGAAAGAAAATTTGGAAAG
CATGGTGGAACTATTCCCATTGTACCCACGGCAGAGTTCCAAGACAGGATATCGGGTGCA
TCTGAGAAAGACATCGTGCACTCTGGCTTGGCATACACAATGGAGCGTTCTGCCAGGCAA
ATTATGCGCACAGCCATGAAGTATAACCTGGGATTGGACCTGAGAACAGCTGCCTATGTT
AATGCCATTGAGAAAGTCTTCAAAGTGTACAATGAAGCTGGTGTGACCTTCACATAG

1. Nakatani Y, Banner C, von Herrath M, Schneider ME, Smith HH, Freese E: Comparison of human brain and liver glutamate dehydrogenase cDNAS. Biochem Biophys Res Commun. 1987 Dec 16;149(2):405-10. [PubMed ]
2. Amuro N, Yamaura M, Goto Y, Okazaki T: Molecular cloning and nucleotide sequence of the cDNA for human liver glutamate dehydrogenase precursor. Biochem Biophys Res Commun. 1988 May 16;152(3):1395-400. [PubMed ]
3. Nakatani Y, Schneider M, Banner C, Freese E: Complete nucleotide sequence of human glutamate dehydrogenase cDNA. Nucleic Acids Res. 1988 Jul 11;16(13):6237. [PubMed ]
4. Mavrothalassitis G, Tzimagiorgis G, Mitsialis A, Zannis V, Plaitakis A, Papamatheakis J, Moschonas N: Isolation and characterization of cDNA clones encoding human liver glutamate dehydrogenase: evidence for a small gene family. Proc Natl Acad Sci U S A. 1988 May;85(10):3494-8. [PubMed ]
5. Michaelidis TM, Tzimagiorgis G, Moschonas NK, Papamatheakis J: The human glutamate dehydrogenase gene family: gene organization and structural characterization. Genomics. 1993 Apr;16(1):150-60. [PubMed ]
6. Julliard JH, Smith EL: Partial amino acid sequence of the glutamate dehydrogenase of human liver and a revision of the sequence of the bovine enzyme. J Biol Chem. 1979 May 10;254(9):3427-38. [PubMed ]
7. Hochstrasser DF, Frutiger S, Paquet N, Bairoch A, Ravier F, Pasquali C, Sanchez JC, Tissot JD, Bjellqvist B, Vargas R, et al.: Human liver protein map: a reference database established by microsequencing and gel comparison. Electrophoresis. 1992 Dec;13(12):992-1001. [PubMed ]
8. Banner C, Silverman S, Thomas JW, Lampel KA, Vitkovic L, Huie D, Wenthold RJ: Isolation of a human brain cDNA for glutamate dehydrogenase. J Neurochem. 1987 Jul;49(1):246-52. [PubMed ]
9. Tzimagiorgis G, Leversha MA, Chroniary K, Goulielmos G, Sargent CA, Ferguson-Smith M, Moschonas NK: Structure and expression analysis of a member of the human glutamate dehydrogenase (GLUD) gene family mapped to chromosome 10p11.2. Hum Genet. 1993 Jun;91(5):433-8. [PubMed ]
10. Smith TJ, Peterson PE, Schmidt T, Fang J, Stanley CA: Structures of bovine glutamate dehydrogenase complexes elucidate the mechanism of purine regulation. J Mol Biol. 2001 Mar 23;307(2):707-20. [PubMed ]
11. Fang J, Hsu BY, MacMullen CM, Poncz M, Smith TJ, Stanley CA: Expression, purification and characterization of human glutamate dehydrogenase (GDH) allosteric regulatory mutations. Biochem J. 2002 Apr 1;363(Pt 1):81-7. [PubMed ]
12. Smith TJ, Schmidt T, Fang J, Wu J, Siuzdak G, Stanley CA: The structure of apo human glutamate dehydrogenase details subunit communication and allostery. J Mol Biol. 2002 May 3;318(3):765-77. [PubMed ]
13. Banerjee S, Schmidt T, Fang J, Stanley CA, Smith TJ: Structural studies on ADP activation of mammalian glutamate dehydrogenase and the evolution of regulation. Biochemistry. 2003 Apr 1;42(12):3446-56. [PubMed ]
14. Meissner T, Beinbrech B, Mayatepek E: Congenital hyperinsulinism: molecular basis of a heterogeneous disease. Hum Mutat. 1999;13(5):351-61. [PubMed ]
15. Stanley CA, Lieu YK, Hsu BY, Burlina AB, Greenberg CR, Hopwood NJ, Perlman K, Rich BH, Zammarchi E, Poncz M: Hyperinsulinism and hyperammonemia in infants with regulatory mutations of the glutamate dehydrogenase gene. N Engl J Med. 1998 May 7;338(19):1352-7. [PubMed ]
16. Miki Y, Taki T, Ohura T, Kato H, Yanagisawa M, Hayashi Y: Novel missense mutations in the glutamate dehydrogenase gene in the congenital hyperinsulinism-hyperammonemia syndrome. J Pediatr. 2000 Jan;136(1):69-72. [PubMed ]
17. Santer R, Kinner M, Passarge M, Superti-Furga A, Mayatepek E, Meissner T, Schneppenheim R, Schaub J: Novel missense mutations outside the allosteric domain of glutamate dehydrogenase are prevalent in European patients with the congenital hyperinsulinism-hyperammonemia syndrome. Hum Genet. 2001 Jan;108(1):66-71. [PubMed ]
18. MacMullen C, Fang J, Hsu BY, Kelly A, de Lonlay-Debeney P, Saudubray JM, Ganguly A, Smith TJ, Stanley CA: Hyperinsulinism/hyperammonemia syndrome in children with regulatory mutations in the inhibitory guanosine triphosphate-binding domain of glutamate dehydrogenase. J Clin Endocrinol Metab. 2001 Apr;86(4):1782-7. [PubMed ]

1. Glutamate decarboxylase 65 kDa isoform
2. GAD-65
3. 65 kDa glutamic acid decarboxylase

MASPGSGFWSFGSEDGSGDSENPGTARAWCQVAQKFTGGIGNKLCALLYGDAEKPAESGG
SQPPRAAARKAACACDQKPCSCSKVDVNYAFLHATDLLPACDGERPTLAFLQDVMNILLQ
YVVKSFDRSTKVIDFHYPNELLQEYNWELADQPQNLEEILMHCQTTLKYAIKTGHPRYFN
QLSTGLDMVGLAADWLTSTANTNMFTYEIAPVFVLLEYVTLKKMREIIGWPGGSGDGIFS
PGGAISNMYAMMIARFKMFPEVKEKGMAALPRLIAFTSEHSHFSLKKGAAALGIGTDSVI
LIKCDERGKMIPSDLERRILEAKQKGFVPFLVSATAGTTVYGAFDPLLAVADICKKYKIW
MHVDAAWGGGLLMSRKHKWKLSGVERANSVTWNPHKMMGVPLQCSALLVREEGLMQNCNQ
MHASYLFQQDKHYDLSYDTGDKALQCGRHVDVFKLWLMWRAKGTTGFEAHVDKCLELAEY
LYNIIKNREGYEMVFDGKPQHTNVCFWYIPPSLRTLEDNEERMSRLSKVAPVIKARMMEY
GTTMVSYQPLGDKVNFFRMVISNPAATHQDIDFLIEEIERLGQDL

• Beta Alanine Metabolism (map00410 )
• Butyrate Metabolism (map00650 )
• Glutamate Metabolism (map00251 )
• Taurine and Hypotaurine Metabolism (map00430 )

• L-glutamate = 4-aminobutanoate + CO2

• Pyridoxal_deC (PF00282 )

• None

• None

ATGGCATCTCCGGGCTCTGGCTTTTGGTCTTTCGGGTCGGAAGATGGCTCTGGGGATTCC
GAGAATCCCGGCACAGCGCGAGCCTGGTGCCAAGTGGCTCAGAAGTTCACGGGCGGCATC
GGAAACAAACTGTGCGCCCTGCTCTACGGAGACGCCGAGAAGCCGGCGGAGAGCGGCGGG
AGCCAACCCCCGCGGGCCGCCGCCCGGAAGGCCGCCTGCGCCTGCGACCAGAAGCCCTGC
AGCTGCTCCAAAGTGGATGTCAACTACGCGTTTCTCCATGCAACAGACCTGCTGCCGGCG
TGTGATGGAGAAAGGCCCACTTTGGCGTTTCTGCAAGATGTTATGAACATTTTACTTCAG
TATGTGGTGAAAAGTTTCGATAGATCAACCAAAGTGATTGATTTCCATTATCCTAATGAG
CTTCTCCAAGAATATAATTGGGAATTGGCAGACCAACCACAAAATTTGGAGGAAATTTTG
ATGCATTGCCAAACAACTCTAAAATATGCAATTAAAACAGGGCATCCTAGATACTTCAAT
CAACTTTCTACTGGTTTGGATATGGTTGGATTAGCAGCAGACTGGCTGACATCAACAGCA
AATACTAACATGTTCACCTATGAAATTGCTCCAGTATTTGTGCTTTTGGAATATGTCACA
CTAAAGAAAATGAGAGAAATCATTGGCTGGCCAGGGGGCTCTGGCGATGGGATATTTTCT
CCCGGTGGCGCCATATCTAACATGTATGCCATGATGATCGCACGCTTTAAGATGTTCCCA
GAAGTCAAGGAGAAAGGAATGGCTGCTCTTCCCAGGCTCATTGCCTTCACGTCTGAACAT
AGTCATTTTTCTCTCAAGAAGGGAGCTGCAGCCTTAGGGATTGGAACAGACAGCGTGATT
CTGATTAAATGTGATGAGAGAGGGAAAATGATTCCATCTGATCTTGAAAGAAGGATTCTT
GAAGCCAAACAGAAAGGGTTTGTTCCTTTCCTCGTGAGTGCCACAGCTGGAACCACCGTG
TACGGAGCATTTGACCCCCTCTTAGCTGTCGCTGACATTTGCAAAAAGTATAAGATCTGG
ATGCATGTGGATGCAGCTTGGGGTGGGGGATTACTGATGTCCCGAAAACACAAGTGGAAA
CTGAGTGGCGTGGAGAGGGCCAACTCTGTGACGTGGAATCCACACAAGATGATGGGAGTC
CCTTTGCAGTGCTCTGCTCTCCTGGTTAGAGAAGAGGGATTGATGCAGAATTGCAACCAA
ATGCATGCCTCCTACCTCTTTCAGCAAGATAAACATTATGACCTGTCCTATGACACTGGA
GACAAGGCCTTACAGTGCGGACGCCACGTTGATGTTTTTAAACTATGGCTGATGTGGAGG
GCAAAGGGGACTACCGGGTTTGAAGCGCATGTTGATAAATGTTTGGAGTTGGCAGAGTAT
TTATACAACATCATAAAAAACCGAGAAGGATATGAGATGGTGTTTGATGGGAAGCCTCAG
CACACAAATGTCTGCTTCTGGTACATTCCTCCAAGCTTGCGTACTCTGGAAGACAATGAA
GAGAGAATGAGTCGCCTCTCGAAGGTGGCTCCAGTGATTAAAGCCAGAATGATGGAGTAT
GGAACCACAATGGTCAGCTACCAACCCTTGGGAGACAAGGTCAATTTCTTCCGCATGGTC
ATCTCAAACCCAGCGGCAACTCACCAAGACATTGACTTCCTGATTGAAGAAATAGAACGC
CTTGGACAAGATTTATAA

1. Karlsen AE, Hagopian WA, Grubin CE, Dube S, Disteche CM, Adler DA, Barmeier H, Mathewes S, Grant FJ, Foster D, et al.: Cloning and primary structure of a human islet isoform of glutamic acid decarboxylase from chromosome 10. Proc Natl Acad Sci U S A. 1991 Oct 1;88(19):8337-41. [PubMed ]
2. Bu DF, Erlander MG, Hitz BC, Tillakaratne NJ, Kaufman DL, Wagner-McPherson CB, Evans GA, Tobin AJ: Two human glutamate decarboxylases, 65-kDa GAD and 67-kDa GAD, are each encoded by a single gene. Proc Natl Acad Sci U S A. 1992 Mar 15;89(6):2115-9. [PubMed ]
3. Bu DF, Tobin AJ: The exon-intron organization of the genes (GAD1 and GAD2) encoding two human glutamate decarboxylases (GAD67 and GAD65) suggests that they derive from a common ancestral GAD. Genomics. 1994 May 1;21(1):222-8. [PubMed ]
4. Mauch L, Abney CC, Berg H, Scherbaum WA, Liedvogel B, Northemann W: Characterization of a linear epitope within the human pancreatic 64-kDa glutamic acid decarboxylase and its autoimmune recognition by sera from insulin-dependent diabetes mellitus patients. Eur J Biochem. 1993 Mar 1;212(2):597-603. [PubMed ]
5. Kim J, Richter W, Aanstoot HJ, Shi Y, Fu Q, Rajotte R, Warnock G, Baekkeskov S: Differential expression of GAD65 and GAD67 in human, rat, and mouse pancreatic islets. Diabetes. 1993 Dec;42(12):1799-808. [PubMed ]
6. Namchuk M, Lindsay L, Turck CW, Kanaani J, Baekkeskov S: Phosphorylation of serine residues 3, 6, 10, and 13 distinguishes membrane anchored from soluble glutamic acid decarboxylase 65 and is restricted to glutamic acid decarboxylase 65alpha. J Biol Chem. 1997 Jan 17;272(3):1548-57. [PubMed ]
7. Kanaani J, el-Husseini Ael-D, Aguilera-Moreno A, Diacovo JM, Bredt DS, Baekkeskov S: A combination of three distinct trafficking signals mediates axonal targeting and presynaptic clustering of GAD65. J Cell Biol. 2002 Sep 30;158(7):1229-38. [PubMed ]

1. Glutamate decarboxylase 67 kDa isoform
2. GAD-67
3. 67 kDa glutamic acid decarboxylase

MASSTPSSSATSSNAGADPNTTNLRPTTYDTWCGVAHGCTRKLGLKICGFLQRTNSLEEK
SRLVSAFKERQSSKNLLSCENSDRDARFRRTETDFSNLFARDLLPAKNGEEQTVQFLLEV
VDILLNYVRKTFDRSTKVLDFHHPHQLLEGMEGFNLELSDHPESLEQILVDCRDTLKYGV
RTGHPRFFNQLSTGLDIIGLAGEWLTSTANTNMFTYEIAPVFVLMEQITLKKMREIVGWS
SKDGDGIFSPGGAISNMYSIMAARYKYFPEVKTKGMAAVPKLVLFTSEQSHYSIKKAGAA
LGFGTDNVILIKCNERGKIIPADFEAKILEAKQKGYVPFYVNATAGTTVYGAFDPIQEIA
DICEKYNLWLHVDAAWGGGLLMSRKHRHKLNGIERANSVTWNPHKMMGVLLQCSAILVKE
KGILQGCNQMCAGYLFQPDKQYDVSYDTGDKAIQCGRHVDIFKFWLMWKAKGTVGFENQI
NKCLELAEYLYAKIKNREEFEMVFNGEPEHTNVCFWYIPQSLRGVPDSPQRREKLHKVAP
KIKALMMESGTTMVGYQPQGDKANFFRMVISNPAATQSDIDFLIEEIERLGQDL

• Beta Alanine Metabolism (map00410 )
• Butyrate Metabolism (map00650 )
• Glutamate Metabolism (map00251 )
• Taurine and Hypotaurine Metabolism (map00430 )

• L-glutamate = 4-aminobutanoate + CO2

• Pyridoxal_deC (PF00282 )

• None

• None

ATGGCGTCTTCGACCCCATCTTCGTCCGCAACCTCCTCGAACGCGGGAGCGGACCCCAAT
ACCACTAACCTGCGCCCCACAACGTACGATACCTGGTGCGGCGTGGCCCATGGATGCACC
AGAAAACTGGGGCTCAAGATCTGCGGCTTCTTGCAAAGGACCAACAGCCTGGAAGAGAAG
AGTCGCCTTGTGAGTGCCTTCAGGGAGAGGCAATCCTCCAAGAACCTGCTTTCCTGTGAA
AACAGCGACCGGGATGCCCGCTTCCGGCGCACAGAGACTGACTTCTCTAATCTGTTTGCT
AGAGATCTGCTTCCGGCTAAGAACGGTGAGGAGCAAACCGTGCAATTCCTCCTGGAAGTG
GTGGACATACTCCTCAACTATGTCCGCAAGACATTTGATCGCTCCACCAAGGTGCTGGAC
TTTCATCACCCACACCAGTTGCTGGAAGGCATGGAGGGCTTCAACTTGGAGCTCTCTGAC
CACCCCGAGTCCCTGGAGCAGATCCTGGTTGACTGCAGAGACACCTTGAAGTATGGGGTT
CGCACAGGTCATCCTCGATTTTTCAACCAGCTCTCCACTGGATTGGATATTATTGGCCTA
GCTGGAGAATGGCTGACATCAACGGCCAATACCAACATGTTTACATATGAAATTGCACCA
GTGTTTGTCCTCATGGAACAAATAACACTTAAGAAGATGAGAGAGATAGTTGGATGGTCA
AGTAAAGATGGTGATGGGATATTTTCTCCTGGGGGCGCCATATCCAACATGTACAGCATC
ATGGCTGCTCGCTACAAGTACTTCCCGGAAGTTAAGACAAAGGGCATGGCGGCTGTGCCT
AAACTGGTCCTCTTCACCTCAGAACAGAGTCACTATTCCATAAAGAAAGCTGGGGCTGCA
CTTGGCTTTGGAACTGACAATGTGATTTTGATAAAGTGCAATGAAAGGGGGAAAATAATT
CCAGCTGATTTTGAGGCAAAAATTCTTGAAGCCAAACAGAAGGGATATGTTCCCTTTTAT
GTCAATGCAACTGCTGGCACGACTGTTTATGGAGCTTTTGATCCGATACAAGAGATTGCA
GATATATGTGAGAAATATAACCTTTGGTTGCATGTCGATGCTGCCTGGGGAGGTGGGCTG
CTCATGTCCAGGAAGCACCGCCATAAACTCAACGGCATAGAAAGGGCCAACTCAGTCACC
TGGAACCCTCACAAGATGATGGGCGTGCTGTTGCAGTGCTCTGCCATTCTCGTCAAGGAA
AAGGGTATACTCCAAGGATGCAACCAGATGTGTGCAGGATATCTCTTCCAGCCAGACAAG
CAGTATGATGTCTCCTACGACACCGGGGACAAGGCAATTCAGTGTGGCCGCCACGTGGAT
ATCTTCAAGTTCTGGCTGATGTGGAAAGCAAAGGGCACAGTGGGATTTGAAAACCAGATC
AACAAATGCCTGGAACTGGCTGAATACCTCTATGCCAAGATTAAAAACAGAGAAGAATTT
GAGATGGTTTTCAATGGCGAGCCTGAGCACACAAACGTCTGTTTTTGGTATATTCCACAA
AGCCTCAGGGGTGTGCCAGACAGCCCTCAACGACGGGAAAAGCTACACAAGGTGGCTCCA
AAAATCAAAGCCCTGATGATGGAGTCAGGTACGACCATGGTTGGCTACCAGCCCCAAGGG
GACAAGGCCAACTTCTTCCGGATGGTCATCTCCAACCCAGCCGCTACCCAGTCTGACATT
GACTTCCTCATTGAGGAGATAGAAAGACTGGGCCAGGATCTGTAA

1. Bu DF, Erlander MG, Hitz BC, Tillakaratne NJ, Kaufman DL, Wagner-McPherson CB, Evans GA, Tobin AJ: Two human glutamate decarboxylases, 65-kDa GAD and 67-kDa GAD, are each encoded by a single gene. Proc Natl Acad Sci U S A. 1992 Mar 15;89(6):2115-9. [PubMed ]
2. Bu DF, Tobin AJ: The exon-intron organization of the genes (GAD1 and GAD2) encoding two human glutamate decarboxylases (GAD67 and GAD65) suggests that they derive from a common ancestral GAD. Genomics. 1994 May 1;21(1):222-8. [PubMed ]
3. Kelly CD, Edwards Y, Johnstone AP, Harfst E, Nogradi A, Nussey SS, Povey S, Carter ND: Nucleotide sequence and chromosomal assignment of a cDNA encoding the large isoform of human glutamate decarboxylase. Ann Hum Genet. 1992 Jul;56(Pt 3):255-65. [PubMed ]
4. Yamashita K, Cram DS, Harrison LC: Molecular cloning of full-length glutamic acid decarboxylase 67 from human pancreas and islets. Biochem Biophys Res Commun. 1993 May 14;192(3):1347-52. [PubMed ]
5. Kawasaki E, Moriuchi R, Watanabe M, Saitoh K, Brunicardi FC, Watt PC, Yamaguchi T, Mullen Y, Akazawa S, Miyamoto T, et al.: Cloning and expression of large isoform of glutamic acid decarboxylase from human pancreatic islet. Biochem Biophys Res Commun. 1993 May 14;192(3):1353-9. [PubMed ]
6. Chessler SD, Lernmark A: Alternative splicing of GAD67 results in the synthesis of a third form of glutamic-acid decarboxylase in human islets and other non-neural tissues. J Biol Chem. 2000 Feb 18;275(7):5188-92. [PubMed ]
7. Cram DS, Barnett LD, Joseph JL, Harrison LC: Cloning and partial nucleotide sequence of human glutamic acid decarboxylase cDNA from brain and pancreatic islets. Biochem Biophys Res Commun. 1991 May 15;176(3):1239-44. [PubMed ]
8. Persson H, Pelto-Huikko M, Metsis M, Soder O, Brene S, Skog S, Hokfelt T, Ritzen EM: Expression of the neurotransmitter-synthesizing enzyme glutamic acid decarboxylase in male germ cells. Mol Cell Biol. 1990 Sep;10(9):4701-11. [PubMed ]

1. Gamma- glutamyltransferase 1
2. GGT 1
3. CD224 antigen[Contains: Gamma- glutamyltranspeptidase 1 heavy chain
4. Gamma-glutamyltranspeptidase 1 light chain]

MKKKLVVLGLLAVVLVLVIVGLCLWLPSASKEPDNHVYTRAAVAADAKQCSKIGRDALRD
GGSAVDAAIAALLCVGLMNAHSMGIGGGLFLTIYNSTTRKAEVINAREVAPRLAFATMFN
SSEQSQKGGLSVAVPGEIRGYELAHQRHGRLPWARLFQPSIQLARQGFPVGKGLAAALEN
KRTVIEQQPVLCEVFCRDRKVLREGERLTLPQLADTYETLAIEGAQAFYNGSLTAQIVKD
IQAAGGIVTAEDLNNYRAELIEHPLNISLGDVVLYMPSAPLSGPVLALILNILKGYNFSR
ESVESPEQKGLTYHRIVEAFRFAYAKRTLLGDPKFVDVTEVVRNMTSEFFAAQLRAQISD
DTTHPISYYKPEFYTPDDGGTAHLSVVAEDGSAVSATSTINLYFGSKVRSPVSGILFNNE
MDDFSSPSITNEFGVPPSPANFIQPGKQPLSSMCPTIMVGQDGQVRMVVGAAGGTQITTA
TALAIIYNLWFGYDVKRAVEEPRLHNQLLPNVTTVERNIDQAVTAALETRHHHTQIASTF
IAVVQAIVRTAGGWAAASDSRKGGEPAGY

• Arachidonic acid metabolism (map00590 )
• Cyanoamino acid metabolism (map00460 )
• Glutathione Metabolism (map00480 )
• Selenoamino Acid Metabolism (map00450 )
• Taurine and Hypotaurine Metabolism (map00430 )

• (5-L-glutamyl)-peptide + an amino acid = peptide + 5-L-glutamyl amino acid

• G_glu_transpept (PF01019 )

• 1-30

ATGAAGAAGAAGTTAGTGGTGCTGGGCCTGCTGGCCGTGGTCCTGGTGCTGGTCATTGTC
GGCCTCTGTCTCTGGCTGCCCTCAGCCTCCAAGGAACCTGACAACCATGTGTACACCAGG
GCTGCCGTGGCCGCGGATGCCAAGCAGTGCTCGAAGATTGGGAGGGATGCACTGCGGGAC
GGTGGCTCTGCGGTGGATGCAGCCATTGCAGCCCTGTTGTGTGTGGGGCTCATGAATGCC
CACAGCATGGGCATCGGGGGTGGCCTCTTCCTCACCATCTACAACAGCACCACACGAAAA
GCTGAGGTCATCAACGCCCGCGAGGTGGCCCCCAGGCTGGCCTTTGCCACCATGTTCAAC
AGCTCGGAGCAGTCCCAGAAGGGGGGGCTGTCGGTGGCGGTGCCTGGGGAGATCCGAGGC
TATGAGCTGGCACACCAGCGGCATGGGCGGCTGCCCTGGGCTCGCCTCTTCCAGCCCAGC
ATCCAGCTGGCCCGCCAGGGCTTCCCCGTGGGCAAGGGCTTGGCGGCAGCCCTGGAAAAC
AAGCGGACCGTCATCGAGCAGCAGCCTGTCTTGTGTGAGGTGTTCTGCCGGGATAGAAAG
GTGCTTCGGGAGGGGGAGAGACTGACCCTGCCGCAGCTGGCTGACACCTACGAGACGCTG
GCCATCGAGGGTGCCCAGGCCTTCTACAACGGCAGCCTCACGGCCCAGATTGTGAAGGAC
ATCCAGGCGGCCGGGGGCATTGTGACAGCTGAGGACCTGAACAACTACCGTGCTGAGCTG
ATCGAGCACCCGCTGAACATCAGCCTGGGAGACGCGGTGCTGTACATGCCCAGTGCGCCG
CTCAGCGGGCCCGTGCTGGCCCTCATCCTCAACATCCTCAAAGGGTACAACTTCTCCCGG
GAGAGCGTGGAGAGCCCCGAGCAGAAGGGCCTGACGTACCACCGCATCGTAGAGGCTTTC
CGGTTTGCCTACGCCAAGAGGACCCTGCTTGGGGACCCCAAGTTTGTGGATGTGACTGAG
GTGGTCCGCAACATGACCTCCGAGTTCTTCGCTGCCCAGCTCCGGGCCCAGATCTCTGAC
GACACCACTCACCCGATCTCCTACTACAAGCCCGAGTTCTACACGCCGGATGACGGGGGC
ACTGCTCACCTGTCTGTCGTCGCAGAGGACGGCAGTGCTGTGTCCGCCACCAGCACCATC
AACCTCTACTTTGGCTCCAAGGTCCGCTCCCCGGTCAGCGGGATCCTGTTCAATAATGAA
ATGGACGACTTCAGCTCTCCCAGCATCACCAACGAGTTTGGGGTACCCCCCTCACCTGCC
AATTTCATCCAGCCAGGGAAGCAGCCGCTCTCGTCCATGTGCCCGACGATCATGGTGGGC
CAGGACGGCCAGGTCCGGATGGTGGTGGGAGCTGCTGGGGGCACACAGATCACCACGGCC
ACTGCACTGGCCATCATCTACAACCTCTGGTTCGGCTATGACGTGAAGCGGGCCGTGGAG
GAGCCCCGGCTGCACAACCAGCTTCTGCCCAACGTCACGACAGTGGAGAGAAACATTGAC
CAGGCAGTGACTGCAGCCCTGGAGACCCGGCACCATCACACCCAGATCGCGTCCACCTTC
ATCGCTGTGGTGCAAGCCATCGTCCGCACGGCTGGTGGCTGGGCAGCTGCCTCGGACTCC
AGGAAAGGCGGGGAGCCTGCCGGCTACTGA

1. Rajpert-De Meyts E, Heisterkamp N, Groffen J: Cloning and nucleotide sequence of human gamma-glutamyl transpeptidase. Proc Natl Acad Sci U S A. 1988 Dec;85(23):8840-4. [PubMed ]
2. Sakamuro D, Yamazoe M, Matsuda Y, Kangawa K, Taniguchi N, Matsuo H, Yoshikawa H, Ogasawara N: The primary structure of human gamma-glutamyl transpeptidase. Gene. 1988 Dec 15;73(1):1-9. [PubMed ]
3. Pitot HC, Goodspeed D, Dunn T, Hendrich S, Maronpot RR, Moran S: Regulation of the expression of some genes for enzymes of glutathione metabolism in hepatotoxicity and hepatocarcinogenesis. Toxicol Appl Pharmacol. 1989 Jan;97(1):23-34. [PubMed ]
4. Goodspeed DC, Dunn TJ, Miller CD, Pitot HC: Human gamma-glutamyl transpeptidase cDNA: comparison of hepatoma and kidney mRNA in the human and rat. Gene. 1989 Mar 15;76(1):1-9. [PubMed ]
5. Pawlak A, Cohen EH, Octave JN, Schweickhardt R, Wu SJ, Bulle F, Chikhi N, Baik JH, Siegrist S, Guellaen G: An alternatively processed mRNA specific for gamma-glutamyl transpeptidase in human tissues. J Biol Chem. 1990 Feb 25;265(6):3256-62. [PubMed ]
6. Courtay C, Oster T, Michelet F, Visvikis A, Diederich M, Wellman M, Siest G: Gamma-glutamyltransferase: nucleotide sequence of the human pancreatic cDNA. Evidence for a ubiquitous gamma-glutamyltransferase polypeptide in human tissues. Biochem Pharmacol. 1992 Jun 23;43(12):2527-33. [PubMed ]
7. Wetmore LA, Gerard C, Drazen JM: Human lung expresses unique gamma-glutamyl transpeptidase transcripts. Proc Natl Acad Sci U S A. 1993 Aug 15;90(16):7461-5. [PubMed ]
8. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed ]
9. Tate SS, Khadse V, Wellner D: Renal gamma-glutamyl transpeptidases: structural and immunological studies. Arch Biochem Biophys. 1988 May 1;262(2):397-408. [PubMed ]
10. Chikhi N, Holic N, Guellaen G, Laperche Y: Gamma-glutamyl transpeptidase gene organization and expression: a comparative analysis in rat, mouse, pig and human species. Comp Biochem Physiol B Biochem Mol Biol. 1999 Apr;122(4):367-80. [PubMed ]
11. Tate SS, Ross ME: Human kidney gamma-glutamyl transpeptidase. Catalytic properties, subunit structure, and localization of the gamma-glutamyl binding site on the light subunit. J Biol Chem. 1977 Sep 10;252(17):6042-5. [PubMed ]
12. Tate SS, Galbraith RA: In vitro translation and processing of human hepatoma cell (Hep G2) gamma-glutamyl transpeptidase. Biochem Biophys Res Commun. 1988 Aug 15;154(3):1167-73. [PubMed ]
13. Ikeda Y, Fujii J, Taniguchi N: Significance of Arg-107 and Glu-108 in the catalytic mechanism of human gamma-glutamyl transpeptidase. Identification by site-directed mutagenesis. J Biol Chem. 1993 Feb 25;268(6):3980-5. [PubMed ]
14. Ikeda Y, Fujii J, Taniguchi N, Meister A: Human gamma-glutamyl transpeptidase mutants involving conserved aspartate residues and the unique cysteine residue of the light subunit. J Biol Chem. 1995 May 26;270(21):12471-5. [PubMed ]
15. Ikeda Y, Fujii J, Anderson ME, Taniguchi N, Meister A: Involvement of Ser-451 and Ser-452 in the catalysis of human gamma-glutamyl transpeptidase. J Biol Chem. 1995 Sep 22;270(38):22223-8. [PubMed ]
16. Ikeda Y, Fujii J, Taniguchi N: Effects of substitutions of the conserved histidine residues in human gamma-glutamyl transpeptidase. J Biochem (Tokyo). 1996 Jun;119(6):1166-70. [PubMed ]

1. Glutathione synthase
2. GSH synthetase
3. GSH-S

MATNWGSLLQDKQQLEELARQAVDRALAEGVLLRTSQEPTSSEVVSYAPFTLFPSLVPSA
LLEQAYAVQMDFNLLVDAVSQNAAFLEQTLSSTIKQDDFTARLFDIHKQVLKEGIAQTVF
LGLNRSDYMFQRSADGSPALKQIEINTISASFGGLASRTPAVHRHVLSVLSKTKEAGKIL
SNNPSKGLALGIAKAWELYGSPNALVLLIAQEKERNIFDQRAIENELLARNIHVIRRTFE
DISEKGSLDQDRRLFVDGQEIAVVYFRDGYMPRQYSLQNWEARLLLERSHAAKCPDIATQ
LAGTKKVQQELSRPGMLEMLLPGQPEAVARLRATFAGLYSLDVGEEGDQAIAEALAAPSR
FVLKPQREGGGNNLYGEEMVQALKQLKDSEERASYILMEKIEPEPFENCLLRPGSPARVV
QCISELGIFGVYVRQEKTLVMNKHVGHLLRTKAIEHADGGVAAGVAVLDNPYPV

• Glutamate Metabolism (map00251 )
• Glutathione Metabolism (map00480 )

• ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione

• GSH_synth_ATP (PF03917 )
• GSH_synthase (PF03199 )

• None

• None

ATGGCCACCAACTGGGGGAGCCTCTTGCAGGATAAACAGCAGCTAGAGGAGCTGGCACGG
CAGGCCGTGGACCGGGCCCTGGCTGAGGGAGTATTGCTGAGGACCTCACAGGAGCCCACT
TCCTCGGAGGTGGTGAGCTATGCCCCATTCACGCTCTTCCCCTCACTGGTCCCCAGTGCC
CTGCTGGAGCAAGCCTATGCTGTGCAGATGGACTTCAACCTGCTAGTGGATGCTGTCAGC
CAGAACGCTGCCTTCCTGGAGCAAACTCTTTCCAGCACCATCAAACAGGATGACTTTACC
GCTCGTCTCTTTGACATCCACAAGCAAGTCCTAAAAGAGGGCATTGCCCAGACTGTGTTC
CTGGGCCTGAATCGCTCAGACTACATGTTCCAGCGCAGCGCAGATGGCTCCCCAGCCCTG
AAACAGATCGAAATCAACACCATCTCTGCCAGCTTTGGGGGCCTGGCCTCCCGGACCCCA
GCTGTGCACCGACATGTTCTCAGTGTCCTGAGTAAGACCAAAGAAGCTGGCAAGATCCTC
TCTAATAATCCCAGCAAGGGACTGGCCCTGGGAATTGCCAAAGCCTGGGAGCTCTACGGC
TCACCCAATGCTCTGGTGCTACTGATTGCTCAAGAGAAGGAAAGAAACATATTTGACCAG
CGTGCCATAGAGAATGAGCTACTGGCCAGGAACATCCATGTGATCCGACGAACATTTGAA
GATATCTCTGAAAAGGGGTCTCTGGACCAAGACCGAAGGCTGTTTGTGGATGGCCAGGAA
ATTGCTGTGGTTTACTTCCGGGATGGCTACATGCCTCGTCAGTACAGTCTACAGAATTGG
GAAGCACGTCTACTGCTGGAGAGGTCACATGCTGCCAAGTGCCCAGACATTGCCACCCAG
CTGGCTGGGACTAAGAAGGTGCAGCAGGAGCTAAGCAGGCCGGGCATGCTGGAGATGTTG
CTCCCTGGCCAGCCTGAGGCTGTGGCCCGCCTCCGCGCCACCTTTGCTGGCCTCTACTCA
CTGGATGTGGGTGAAGAAGGGGACCAGGCCATCGCCGAGGCCCTTGCTGCCCCTAGCCGG
TTTGTGCTAAAGCCCCAGAGAGAGGGTGGAGGTAACAACCTATATGGGGAGGAAATGGTA
CAGGCCCTGAAACAGCTGAAGGACAGTGAGGAGAGGGCCTCCTACATCCTCATGGAGAAG
ATCGAACCTGAGCCTTTTGAGAATTGCCTGCTACGGCCTGGCAGCCCTGCCCGAGTGGTC
CAGTGCATTTCAGAGCTGGGCATCTTTGGGGTCTATGTCAGGCAGGAAAAGACACTCGTG
ATGAACAAGCACGTGGGGCATCTACTTCGAACCAAAGCCATCGAGCATGCAGATGGTGGT
GTGGCAGCGGGAGTGGCAGTCCTGGACAACCCATACCCTGTGTGA

1. Gali RR, Board PG: Sequencing and expression of a cDNA for human glutathione synthetase. Biochem J. 1995 Aug 15;310 ( Pt 1):353-8. [PubMed ]
2. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed ]
3. Shi ZZ, Habib GM, Rhead WJ, Gahl WA, He X, Sazer S, Lieberman MW: Mutations in the glutathione synthetase gene cause 5-oxoprolinuria. Nat Genet. 1996 Nov;14(3):361-5. [PubMed ]
4. Dahl N, Pigg M, Ristoff E, Gali R, Carlsson B, Mannervik B, Larsson A, Board P: Missense mutations in the human glutathione synthetase gene result in severe metabolic acidosis, 5-oxoprolinuria, hemolytic anemia and neurological dysfunction. Hum Mol Genet. 1997 Jul;6(7):1147-52. [PubMed ]

1. Folylpoly-gamma-glutamate synthetase
2. FPGS
3. Tetrahydrofolate synthase
4. Tetrahydrofolylpolyglutamate synthase

MSRARSHLRAALFLAAASARGITTQVAARRGLSAWPVPQEPSMEYQDAVRMLNTLQTNAG
YLEQVKRQRGDPQTQLEAMELYLARSGLQVEDLDRLNIIHVTGTKGKGSTCAFTECILRS
YGLKTGFFSSPHLVQVRERIRINGQPISPELFTKYFWRLYHRLEETKDGSCVSMPPYFRF
LTLMAFHVFLQEKVDLAVVEVGIGGAYDCTNIIRKPVVCGVSSLGIDHTSLLGDTVEKIA
WQKGGIFKQGVPAFTVLQPEGPLAVLRDRAQQISCPLYLCPMLEALEEGGPPLTLGLEGE
HQRSNAALALQLAHCWLQRQDRHGAGEPKASRPGLLWQLPLAPVFQPTSHMRLGLRNTEW
PGRTQVLRRGPLTWYLDGAHTASSAQACVRWFRQALQGRERPSGGPEVRVLLFNATGDRD
PAALLKLLQPCQFDYAVFCPNLTEVSSTGNADQQNFTVTLDQVLLRCLEHQQHWNHLDEE
QASPDLWSAPSPEPGGSASLLLAPHPPHTCSASSLVFSCISHALQWISQGRDPIFQPPSP
PKGLLTHPVAHSGASILREAAAIHVLVTGSLHLVGGVLKLLEPALSQ

• Folate and Pterine Biosynthesis (map00790 )

• ATP + tetrahydrofolyl-[Glu]n + L-glutamate = ADP + phosphate + tetrahydrofolyl-[Glu]n+1

• Mur_ligase_C (PF02875 )

• 1-19

ATGGAGTACCAGGATGCCGTGCGCATGCTCAATACCCTGCAGACCAATGCCGGCTACCTG
GAGCAGGTGAAGCGCCAGCGGGGTGACCCTCAGACACAGTTGGAAGCCATGGAACTGTAC
CTGGCACGGAGTGGGCTGCAGGTGGAGGACTTGGACCGGCTGAACATCATCCACGTCACT
GGGACGAAGGGGAAGGGCTCCACCTGTGCCTTCACGGAATGTATCCTCCGAAGCTATGGC
CTGAAGACGGGATTCTTTAGCTCTCCCCACCTGGTGCAGGTTCGGGAGCGGATCCGCATC
AATGGGCAGCCCATCAGTCCTGAGCTCTTCACCAAGTACTTCTGGCGCCTCTACCACCGG
CTGGAGGAGACCAAGGATGGCAGCTGTGTCTCCATGCCCCCCTACTTCCGCTTCCTGACA
CTCATGGCCTTCCACGTCTTCCTCCAAGAGAAGGTGGACCTGGCAGTGGTGGAGGTGGGC
ATTGGCGGGGCTTATGACTGCACCAACATCATCAGGAAGCCTGTGGTGTGCGGAGTCTCC
TCTCTTGGCATCGACCACACCAGCCTCCTGGGGGATACGGTGGAGAAGATCGCATGGCAG
AAAGGGGGCATCTTTAAGCAAGGTGTCCCTGCCTTCACTGTGCTCCAACCTGAAGGTCCC
CTGGCAGTGCTGAGGGACCGAGCCCAGCAGATCTCATGTCCTCTATACCTGTGTCCGATG
CTGGAGGCCCTCGAGGAAGGGGGGCCGCCGCTGACCCTGGGCCTGGAGGGGGAGCACCAG
CGGTCCAACGCCGCCTTGGCCTTGCAGCTGGCCCACTGCTGGCTGCAGCGGCAGGACCGC
CATGGTGCTGGGGAGCCAAAGGCATCCAGGCCAGGGCTCCTGTGGCAGCTGCCCCTGGCA
CCTGTGTTCCAGCCCACATCCCACATGCGGCTCGGGCTTCGGAACACGGAGTGGCCGGGC
CGGACGCAGGTGCTGCGGCGCGGGCCCCTCACCTGGTACCTGGACGGTGCGCACACCGCC
AGCAGCGCGCAGGCCTGCGTGCGCTGGTTCCGCCAGGCGCTGCAGGGCCGCGAGAGGCCG
AGCGGTGGCCCCGAGGTTCGAGTCTTGCTCTTCAATGCTACCGGGGACCGGGACCCGGCG
GCCCTGCTGAAGCTGCTGCAGCCCTGCCAGTTTGACTATGCCGTCTTCTGCCCTAACCTG
ACAGAGGTGTCATCCACAGGCAACGCAGACCAACAGAACTTCACAGTGACACTGGACCAG
GTCCTGCTCCGCTGCCTGGAACACCAGCAGCACTGGAACCACCTGGACGAAGAGCAGGCC
AGCCCGGACCTCTGGAGTGCCCCCAGCCCAGAGCCCGGTGGGTCCGCATCCCTGCTTCTG
GCGCCCCACCCACCCCACACCTGCAGTGCCAGCTCCCTCGTCTTCAGCTGCATTTCACAT
GCCTTGCAATGGATCAGCCAAGGCCGAGACCCCATCTTCCAGCCACCTAGTCCCCCAAAG
GGCCTCCTCACCCACCCTGTGGCTCACAGTGGGGCCAGCATACTCCGTGAGGCTGCTGCC
ATCCATGTGCTAGTCACTGGCAGCCTGCACCTGGTGGGTGGTGTCCTGAAGCTGCTGGAG
CCCGCACTGTCCCAGTAG

1. Garrow TA, Admon A, Shane B: Expression cloning of a human cDNA encoding folylpoly(gamma-glutamate) synthetase and determination of its primary structure. Proc Natl Acad Sci U S A. 1992 Oct 1;89(19):9151-5. [PubMed ]
2. Freemantle SJ, Taylor SM, Krystal G, Moran RG: Upstream organization of and multiple transcripts from the human folylpoly-gamma-glutamate synthetase gene. J Biol Chem. 1995 Apr 21;270(16):9579-84. [PubMed ]
3. Taylor SM, Freemantle SJ, Moran RG: Structural organization of the human folypoly-gamma-glutamate synthetase gene: evidence for a single genomic locus. Cancer Res. 1995 Dec 15;55(24):6030-4. [PubMed ]
4. Cichowicz DJ, Shane B: Mammalian folylpoly-gamma-glutamate synthetase. 1. Purification and general properties of the hog liver enzyme. Biochemistry. 1987 Jan 27;26(2):504-12. [PubMed ]

1. P5CS
2. Aldehyde dehydrogenase 18 family member A1[Includes: Glutamate 5-kinase
3. Gamma-glutamyl kinase
4. GK
5. Gamma-glutamyl phosphate reductase
6. GPR
7. Glutamate-5-semialdehyde dehydrogenase
8. Glutamyl-gamma-semialdehyde dehydrogenase]

MLSQVYRCGFQPFNQHLLPWVKCTTVFRSHCIQPSVIRHVRSWSNIPFITVPLSRTHGKS
FAHRSELKHAKRIVVKLGSAVVTRGDECGLALGRLASIVEQVSVLQNQGREMMLVTSGAV
AFGKQRLRHEILLSQSVRQALHSGQNQLKEMAIPVLEARACAAAGQSGLMALYEAMFTQY
SICAAQILVTNLDFHDEQKRRNLNGTLHELLRMNIVPIVNTNDAVVPPAEPNSDLQGVNV
ISVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPGSDDAKLIDIFYPGDQQSVTFGTK
SRVGMGGMEAKVKAALWALQGGTSVVIANGTHPKVSGHVITDIVEGKKVGTFFSEVKPAG
PTVEQQGEMARSGGRMLATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLEEAEGRLAA
PLLKRLSLSTSKLNSLAIGLRQIAASSQDSVGRVLRRTRIAKNLELEQVTVPIGVLLVIF
ESRPDCLPQVAALAIASGNGLLLKGGKEAAHSNRILHLLTQEALSIHGVKEAVQLVNTRE
EVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKGIPVMGHSEGICHMYVDSEASVDKVTRL
VRDSKCEYPAACNALETLLIHRDLLRTPLFDQIIDMLRVEQVKIHAGPKFASYLTFSPSE
VKSLRTEYGDLELCIEVVDNVQDAIDHIHKYGSSHTDVIVTEDENTAEFFLQHVDSACVF
WNASTRFSDGYRFGLGAEVGISTSRIHARGPVGLEGLLTTKWLLRGKDHVVSDFSEHGSL
KYLHENLPIPQRNTN

• ATP + L-glutamate = ADP + L-glutamate 5-phosphate

• AA_kinase (PF00696 )

• None

• None

ATGTTGAGTCAAGTTTACCGCTGTGGGTTCCAGCCCTTCAACCAACATCTTCTGCCCTGG
GTCAAGTGTACAACCGTCTTCAGATCTCATTGTATCCAGCCTTCAGTCATCAGACATGTT
CGTTCTTGGAGCAACATCCCGTTTATCACTGTACCCCTCAGTCGTACACATGGCAAGTCC
TTCGCCCACCGCAGTGAGCTGAAGCATGCCAAGAGAATCGTGGTGAAGCTCGGCAGTGCC
GTGGTGACCCGAGGGGATGAATGTGGCCTGGCCCTGGGGCGCTTGGCATCTATTGTTGAG
CAGGTATCAGTGCTGCAGAATCAGGGCAGAGAGATGATGCTGGTGACCAGTGGAGCCGTA
GCCTTTGGCAAACAAACGTTGCGCCATGAGATCCTTCTGTCTCAGAGCGTGCGGCAGGCC
CTCCACTCGGGGCAGAACCAGCTGAAAGAAATGGCAATTCCAGTCTTAGAGGCACGAGCC
TGTGCAGCTGCCGGACAGAGTGGGCTGATGGCCTTGTATGAGGCTATGTTTACCCAGTAC
AGCATCTGTGCTGCCCAGATTTTGGTGACCAATTTGGATTTCCATGATGAGCAGAAGCGC
CGGAACCTCAATGGAACACTTCATGAACTCCTTAGAATGAACATTGTCCCCATTGTCAAC
ACAAATGATGCTGTTGTCCCCCCAGCTGAGCCCAACAGTGACCTGCAGGGGGTAAATGTT
ATTAGTGTTAAAGATAATGATAGCCTGGCTGCCCGACTGGCTGTGGAAATGAAAACTGAT
CTCTTGATTGTCCTTCCAGATGTAGAAGGCCTTTTTGACAGCCCCCCAGGTTCAGATGAT
GCAAAGCTTATTGATATATTTTATCCCGGAGATCAGCAGTCTGTGACATTTGGACCCAAG
TCTAGAGTGGGAAATGGGTGCATGGAAGCCAAGGTGAAAAGCACCCTCTGGGCTTTGCAA
GGTGGCACTTCTGTTGTTATTGCCAATGGAACCCACCCAAAGGTGTCTGGGCACGTCATC
ACAGACATTGTGGAGGGGAAGAAAGTTGGTACCTTCTTTTCAGAAGTAAAGCCTGCAGGC
CCTACTGTTGAGCAGCAGGGAGAAATGGCGCGATCTGGAGGAAGGATGTTGGCCACCTTG
GAACCTGAGCAGAGAGCAGAAATTATCCATCATCTGGCTGATCTGTTGACGGACCAGCGT
GATGAGATCCTGTTAGCCAACAAAAAAGACTTGGAGGAGGCAGAGGGGAGACTTGCAGCT
CCTCTGCTGAAACGTTTAAGCCTCTCCACATCCAAATTGAACAGCCTGGCCATCGGTCTG
CGACAGATCGCAGCCTCCTCCCAGGACAGCGTGGGACGTGTTTTGCGCCGCACCCGAATC
GCCAAAAACTTGGAACTGGAACAAGTGACTGTCCCAATTGGAGTTCTGCTGGTGATCTTT
GAATCTCGTCCTGACTGTCCTACCCCAGGTGGCAGCTTTGCTATCGCAAGTGGCAATGGC
TTGTTACTCAAAGGAGGGAAGGAGGCTGCACACAGCAACCGGATTCTCCACCTCCTGACC
CAGGAGGCTCTCTCAATCCATGGAGTCAAGGAGGCCGTGCAACTGGTGAATACCAGAGAA
GAAGTTGAAGATCTTTGCCGCCTAGACAAAATGATAGATCTGATCATTCCACGTGGCTCT
TCCCAGCTGGTCAGAGACATCCAGAAAGCTGCTAAGGGGATTCCAGTGATGGGGCACAGC
GAAGGGATCTGTCACATGTATGTGGATTCCGAGGCCAGTGTTGATAAGGTCACCAGGCTA
GTCAGAGACTCTAAATGTGAATATCCAGCTGCCTGTAATGCTTTGGAGACTTTGTTAATC
CACCGGGATCTGCTCAGGACACCATTATTTGACCAGATCATTGATATGCTGAGAGTGGAA
CAGGTAAAAATTCATGCAGGCCCCAAATTTGCCTCCTATCTGACCTTCAGCCCCTCCGAA
GTGAAGTCACTCCGAACTGAGTATGGGGACCTGGAATTATGCATTGAAGTAGTGGACAAC
GTTCAGGATGCCATTGACCACATCCACAAGTATGGCAGCTCCCACACGGATGTCATCGTC
ACAGAGGACGAAAACACAGCGGAGTTCTTCCTGCAGCACGTAGACAGTGCCTGTGTGTTC
TGGAATGCCAGCACTCGCTTTTCTGATGGTTACCGCTTTGGACTGGGAGCTGAAGTGGGA
ATCAGTACATCGAGAATCCACGCCCGGGGACCAGTAGGACTTGAGGGACTGCTTACTACT
AAGTGGCTGCTGCGAGGGAAGGACCACGTGGTCTCAGATTTCTCAGAGCATGGAAGTTTA
AAATATCTTCATGAGAACCTCCCTATTCCTCAGAGAAACACCAACTGA

1. Aral B, Schlenzig JS, Liu G, Kamoun P: Database cloning human delta 1-pyrroline-5-carboxylate synthetase (P5CS) cDNA: a bifunctional enzyme catalyzing the first 2 steps in proline biosynthesis. C R Acad Sci III. 1996 Mar;319(3):171-8. [PubMed ]
2. Hu CA, Lin WW, Obie C, Valle D: Molecular enzymology of mammalian Delta1-pyrroline-5-carboxylate synthase. Alternative splice donor utilization generates isoforms with different sensitivity to ornithine inhibition. J Biol Chem. 1999 Mar 5;274(10):6754-62. [PubMed ]

1. 5-oxo-L-prolinase
2. Pyroglutamase
3. 5- OPase

MGSPEGRFHFAIDRGGTFTDVFAQCPGGHVRVLKLLSEDPANYADAPTEGIRRILEQEAG
MLLPRDQPLDSSHIASIRMGTTVATNALLERKGERVALLVTRGFRDLLHIGTQARGDLFD
LAVPMPEVLYEEVLEVDERVVLHRGEAGTGTPVKGRTGDLLEVQQPVDLGALRGKLEGLL
SRGIRSLAVVLMHSYTWAQHEQQVGVLARELGFTHVSLSSEAMPMVRIVPRGHTACADAY
LTPAIQRYVQGFCRGFQGQLKDVQVLFMRSDGGLAPMDTFSGSSAVLSGPAGGVVGYSAT
TYQQEGGQPVIGFDMGGTSTDVSRYAGEFEHVFEASTAGVTLQAPQLDINTVAAGGGSRL
FFRSGLFVVGPESAGAHPGPACYRKGGPVTVTDANLVLGRLLPASFPCIFGPGENQPLSP
EASRKALEAVATEVNSFLTNGPCPASPLSLEEVAMGFVRVANEAMCRPIRALTQARGHDP
SAHVLACFGGAGGQHACAIARALGMDTVHIHRHSGLLSALGLALADVVHEAQEPCSLLYA
PETFVQLDQRLSRLEEQCVDALQAQGFPRSQISTESFLHLRYQGTDCALMVSAHQHPATA
RSPRAGDFGAAFVERYMREFGFVIPERPVVVDDVRVRGTGRSGLRLEDAPKAQTGPPRVD
KMTQCYFEGGYQETPVYLLAELGYGHKLHGPCLIIDSNSTILVEPGCQAEVTKTGDICIS
VGAEVPGTVGPQLDPIQLSIFSHRFMSIAEQMGRILQRTAISTNIKERLDFSCALFGPDG
GLVSNAPHIPVHLGAMQETVQFQIQHLGADLHPGDVLLSNHPSAGGSHLPDLTVITPVFW
PGQTRPVFYVASRGHHADIGGITPGSMPPHSTMLQQEGAVFLSFKLVQGGVFQEEAVTEA
LRAPGKVPNCSGTRNLHDNLSDLRAQVAANQKGIQLVGELIGQYGLDVVQAYMGHIQANA
ELAVRDMLRAFGTSRQARGLPLEVSSEDHMDDGSPIRLRVQISLSQGSAVFDFSGTGPEV
FGNLNAPRAVTLSALIYCLRCLVGRDIPLNQGCLAPVRVVIPRGSILDPSPEAAVVGGNV
LTSQRVVDVILGAFGACAASQGCMNNVTLGNAHMGYYETVAGGAGAGPSWHGRSGVHSHM
TNTRITDPEILESRYPVILRRFELRRGSGGRGRFRGGDGVTRELLFREEALLSVLTERRA
FRPYGLHGGEPGARGLNLLIRKNGRTVNLGGKTSVTVYPGDVFCLHTPGGGGYGDPEDPA
PPPGSPPQALAFPEHGSVYEYRRAQEAV

• Glutathione Metabolism (map00480 )

• ATP + 5-oxo-L-proline + 2 H2O = ADP + phosphate + L-glutamate

• Hydant_A_N (PF05378 )
• Hydantoinase_A (PF01968 )
• Hydantoinase_B (PF02538 )

• None

• None

ATGGGCAGCCCCGAGGGCCGCTTCCACTTTGCCATCGACCGTGGGGGTACCTTCACAGAC
GTCTTTGCCCAGTGCCCAGGGGGGCACGTGCGGGTCTTAAAACTGCTCTCAGAGGACCCT
GCCAACTATGCGGACGCGCCAACCGAAGGCATCCGCCGCATCCTGGAGCAGGAGGCCGGC
ATGCTCCTGCCCCGGGACCAGCCGCTGGACTCCAGTCATATCGCCAGCATCCGCATGGGC
ACCACAGTGGCCACCAACGCACTGCTGGAGCGGAAGGGGGAGCGGGTGGCGCTGCTGGTG
ACACGTGGCTTCCGAGACCTGCTGCACATTGGCACCCAAGCCCGTGGGGACCTCTTTGAC
CTGGCCGTGCCCATGCCTGAGGTGCTGTATGAAGAGGTGCTGGAGGTGGACGAACGCGTG
GTGCTGCACCGTGGAGAGGCGGGCACCGGGACGCCTGTGAAAGGCCGCACGGGGGACCTG
CTGGAAGTGCAGCAGCCTGTGGACCTGGGGGCCCTGCGTGGGAAGCTGGAGGGGCTGCTA
TCTCGAGGCATCCGCAGCCTGGCTGTGGTGCTCATGCACTCGTACACGTGGGCCCAGCAT
GAGCAGCAGGTGGGTGTGCTGGCCCGGGAGCTGGGCTTCACGCACGTGTCACTGTCCTCG
GAGGCCATGCCCATGGTGCGCATCGTCCCTCGGGGGCACACGGCCTGTGCCGACGCCTAC
CTCACGCCCGCCATCCAGCGCTACGTGCAGGGCTTCTGCCGTGGCTTCCAGGGCCAACTC
AAGGATGTGCAGGTGTTGTTCATGCGCTCCGATGGCGGCCTGGCGCCCATGGACACCTTC
AGCGGCTCCAGTGCTGTGCTCTCGGGCCCGGCCGGCGGCGTGGTGGGCTACTCAGCCACC
ACCTACCAGCAGGAGGGTGGCCAGCCTGTCATCGGCTTTGACATGGGAGGCACGTCCACG
GATGTGAGCCGCTATGCTGGGGAATTCGAGCACGTCTTCGAGGCCAGCACAGCTGGCGTC
ACCCTCCAGGCCCCGCAGCTGGACATCAACACCGTGGCAGCGGGAGGGGGTTCCCGCCTC
TTCTTCAGGTCTGGCCTCTTTGTGGTTGGGCCCGAGTCAGCAGGAGCCCACCCAGGACCC
GCCTGCTACCGCAAAGGGGGCCCTGTGACAGTGACGGATGCTAATCTGGTCCTGGGTCGC
CTGCTGCCTGCCTCCTTCCCCTGCATTTTTGGGCCGGGAGAGAACCAACCACTTTCCCCT
GAGGCCTCCCGCAAAGCCCTGGAGGCTGTGGCCACTGAGGTCAACAGCTTCCTGACCAAC
GGGCCCTGCCCGGCCTCCCCGCTGAGCCTGGAGGAGGTGGCCATGGGGTTCGTGCGCGTG
GCCAACGAGGCCATGTGCCGGCCCATCCGTGCACTCACGCAGGCAAGAGGCCATGACCCC
TCAGCCCATGTGCTGGCCTGCTTTGGGGGAGCTGGTGGGCAGCATGCATGTGCCATCGCC
CGGGCCCTGGGCATGGACACGGTGCACATCCACAGGCACAGTGGGCTGCTGTCGGCCCTG
GGGCTGGCCCTGGCTGACGTGGTGCATGAGGCACAGGAACCCTGCTCCCTGCTCTACGCG
CCTGAGACCTTCGTGCAGCTGGACCAGAGGCTGAGCCGCCTGGAGGAGCAGTGTGTGGAT
GCTCTGCAGGCCCAGGGCTTCCCCAGGTCCCAGATCAGCACTGAGAGCTTCCTGCACCTG
CGCTACCAGGGCACGGACTGTGCTCTGATGGTGTCTGCCCACCAGCACCCAGCCACAGCC
CGCTCGCCCCGTGCGGGGGACTTCGGGGCAGCCTTTGTGGAGCGGTACATGAGGGAGTTT
GGCTTTGTCATACCTGAGCGGCCGGTGGTCGTGGACGATGTGCGAGTGCGGGGCACCGGC
CGCAGTGGTCTTCGCCTCGAGGATGCCCCCAAAGCCCAGACCGGGCCTCCCCGGGTGGAC
AAGATGACCCAGTGCTACTTTGAGGGGGGCTACCAGGAGACCCCTGTGTACCTGCTGGCA
GAGCTGGGCTATGGGCACAAGCTCCATGGGCCCTGCCTCATCATCGACAGTAACAGCACC
ATCCTGGTGGAGCCAGGTTGCCAGGCAGAGGTGACCAAGACAGGGGACATCTGCATCTCC
GTGGGGGCCGAAGTCCCCGGCACAGTGGGCCCCCAGCTGGACCCTATCCAGCTGTCCATC
TTCTCACACCGCTTCATGAGCATTGCTGAGCAGATGGGCCGCATCCTGCAGCGCACAGCC
ATCTCCACCAACATCAAGGAGCGTCTGGACTTCTCCTGTGCCCTCTTTGGGCCCGATGGG
GGGCTGGTGTCCAATGCCCCCCACATCCCTGTGCACCTGGGTGCCATGCAGGAGACGGTG
CAGTTCCAGATTCAGCACCTGGGGGCCGATCTCCACCCTGGCGACGTGCTACTGAGCAAC
CATCCCAGTGCCGGGGGCAGCCACCTGCCAGACCTGACTGTTATCACACCGGTGTTTTGG
CCGGGTCAGACGCGGCCTGTGTTCTATGTGGCCAGCCGAGGGCACCACGCAGACATCGGG
GGCATCACACCAGGCTCCATGCCCCCCCACTCCACCATGCTGCAACAGGAGGGTGCCGTC
TTTCTGTCCTTCAAACTTGTCCAGGGGGGCGTCTTCCAGGAGGAGGCGGTGACGGAGGCC
CTGCGGGCGCCAGGCAAGGTCCCCAACTGCAGCGGAACCAGAAACCTGCACGACAACCTG
TCGGACCTCCGTGCCCAGGTGGCAGCCAACCAGAAGGGCATCCAGCTGGTGGGGGAGCTC
ATTGGGCAGTACGGCCTGGACGTGGTGCAGGCCTACATGGGCCATATTCAGGCAAACGCT
GAGCTGGCCGTGCGAGACATGTTGCGTGCCTTTGGAACCTCCCGGCAGGCCCGGGGCCTG
CCCCTGGAGGTGTCCTCGGAAGACCACATGGACGACGGTTCCCCCATCCGCCTCCGTGTG
CAGATCAGCCTGAGTCAGGGCAGCGCTGTGTTTGACTTCAGCGGCACTGGGCCGGAGGTG
TTTGGTAATCTCAACGCACCGCGGGCCGTAACCCTGTCCGCCCTCATCTACTGCCTGCGC
TGTCTGGTGGGCCGCGACATCCCACTCAACCAGGGCTGCCTGGCGCCAGTGCGCGTGGTC
ATTCCCCGAGGCTCCATCCTGGACCCGTCGCCCGAGGCGGCGGTGGTGGGCGGCAACGTG
CTCACGTCGCAGCGCGTGGTGGATGTCATCCTGGGGGCCTTTGGGGCCTGCGCCGCCTCC
CAGGGCTGCATGAACAACGTGACCCTGGGCAACGCCCACATGGGCTACTACGAGACGGTG
GCGGGCGGCGCGGGCGCGGGTCCCAGCTGGCACGGGCGCAGCGGTGTGCACAGCCACATG
ACCAACACACGCATCACCGACCCTGAGATCCTGGAGAGCCGGTACCCGGTCATCCTGCGC
CGCTTCGAGCTGCGGCGGGGCTCGGGGGGCAGAGGCCGCTTCCGAGGCGGCGACGGCGTC
ACCCGCGAGCTGCTCTTTCGTGAGGAGGCGCTGCTGTCAGTGCTGACCGAGCGCCGCGCC
TTCCGGCCATACGGGCTCCACGGGGGCGAGCCTGGCGCCCGCGGCCTAAACCTGCTGATC
CGCAAAAACGGCCGGACGGTGAATCTGGGCGGCAAGACGTCGGTGACCGTGTACCCCGGG
GATGTGTTCTGTCTCCACACGCCCGGCGGCGGTGGCTATGGGGACCCGGAGGACCCCGCC
CCACCGCCGGGGTCGCCCCCGCAAGCACTGGCCTTTCCCGAGCACGGCAGCGTCTATGAG
TATCGCCGGGCCCAGGAGGCCGTGTGA

1. N-methyl-D- aspartate receptor subunit NR1

MSTMRLLTLALLFSCSVARAACDPKIVNIGAVLSTRKHEQMFREAVNQANKRHGSWKIQL
NATSVTHKPNAIQMALSVCEDLISSQVYAILVSHPPTPNDHFTPTPVSYTAGFYRIPVLG
LTTRMSIYSDKSIHLSFLRTVPPYSHQSSVWFEMMRVYSWNHIILLVSDDHEGRAAQKRL
ETLLEERESKAEKVLQFDPGTKNVTALLMEAKELEARVIILSASEDDAATVYRAAAMLNM
TGSGYVWLVGEREISGNALRYAPDGILGLQLINGKNESAHISDAVGVVAQAVHELLEKEN
ITDPPRGCVGNTNIWKTGPLFKRVLMSSKYADGVTGRVEFNEDGDRKFANYSIMNLQNRK
LVQVGIYNGTHVIPNDRKIIWPGGETEKPRGYQMSTRLKIVTIHQEPFVYVKPTLSDGTC
KEEFTVNGDPVKKVICTGPNDTSPGSPRHTVPQCCYGFCIDLLIKLARTMNFTYEVHLVA
DGKFGTQERVNNSNKKEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTI
LVKKEIPRSTLDSFMQPFQSTLWLLVGLSVHVVAVMLYLLDRFSPFGRFKVNSEEEEEDA
LTLSSAMWFSWGVLLNSGIGEGAPRSFSARILGMVWAGFAMIIVASYTANLAAFLVLDRP
EERITGINDPRLRNPSDKFIYATVKQSSVDIYFRRQVELSTMYRHMEKHNYESAAEAIQA
VRDNKLHAFIWDSAVLEFEASQKCDLVTTGELFFRSGFGIGMRKDSPWKQNVSLSILKSH
ENGFMEDLDKTWVRYQECDSRSNAPATLTFENMAGVFMLVAGGIVAGIFLIFIEIAYKRH
KDARRKQMQLAFAAVNVWRKNLQDRKSGRAEPDPKKKATFRAITSTLASSFKRRRSSKDT
STGGGRGALQNQKDTVLPRRAIEREEGQLQLCSRHRES

• ANF_receptor (PF01094 )
• Lig_chan (PF00060 )

• 1-18

• 560-580 637-657 813-833

ATGAGCACCATGCGCCTGCTGACGCTCGCCCTGCTGTTCTCCTGCTCCGTCGCCCGTGCC
GCGTGCGACCCCAAGATCGTCAACATTGGCGCGGTGCTGAGCACGCGGAAGCACGAGCAG
ATGTTCCGCGAGGCCGTGAACCAGGCCAACAAGCGGCACGGCTCCTGGAAGATTCAGCTC
AATGCCACCTCCGTCACGCACAAGCCCAACGCCATCCAGATGGCTCTGTCGGTGTGCGAG
GACCTCATCTCCAGCCAGGTCTACGCCATCCTAGTTAGCCATCCACCTACCCCCAACGAC
CACTTCACTCCCACCCCTGTCTCCTACACAGCCGGCTTCTACCGCATACCCGTGCTGGGG
CTGACCACCCGCATGTCCATCTACTCGGACAAGAGCATCCACCTGAGCTTCCTGCGCACC
GTGCCGCCCTACTCCCACCAGTCCAGCGTGTGGTTTGAGATGATGCGTGTCTACAGCTGG
AACCACATCATCCTGCTGGTCAGCGACGACCACGAGGGCCGGGCGGCTCAGAAACGCCTG
GAGACGCTGCTGGAGGAGCGTGAGTCCAAGGCAGAGAAGGTGCTGCAGTTTGACCCAGGG
ACCAAGAACGTGACGGCCCTGCTGATGGAGGCGAAAGAGCTGGAGGCCCGGGTCATCATC
CTTTCTGCCAGCGAGGACGATGCTGCCACTGTATACCGCGCAGCCGCGATGCTGAACATG
ACGGGCTCCGGGTACGTGTGGCTGGTCGGCGAGCGCGAGATCTCGGGGAACGCCCTGCGC
TACGCCCCAGACGGCATCCTCGGGCTGCAGCTCATCAACGGCAAGAACGAGTCGGCCCAC
ATCAGCGACGCCGTGGGCGTGGTGGCCCAGGCCGTGCACGAGCTCCTCGAGAAGGAGAAC
ATCACCGACCCGCCGCGGGGCTGCGTGGGCAACACCAACATCTGGAAGACCGGGCCGCTC
TTCAAGAGAGTGCTGATGTCTTCCAAGTATGCGGATGGGGTGACTGGTCGCGTGGAGTTC
AATGAGGATGGGGACCGGAAGTTCGCCAACTACAGCATCATGAACCTGCAGAACCGCAAG
CTGGTGCAAGTGGGCATCTACAATGGCACCCACGTCATCCCTAATGACAGGAAGATCATC
TGGCCAGGCGGAGAGACAGAGAAGCCTCGAGGGTACCAGATGTCCACCAGACTGAAGATT
GTGACGATCCACCAGGAGCCCTTCGTGTACGTCAAGCCCACGCTGAGTGATGGGACATGC
AAGGAGGAGTTCACAGTCAACGGCGACCCAGTCAAGAAGGTGATCTGCACCGGGCCCAAC
GACACGTCGCCGGGCAGCCCCCGCCACACGGTGCCTCAGTGTTGCTACGGCTTTTGCATC
GACCTGCTCATCAAGCTGGCACGGACCATGAACTTCACCTACGAGGTGCACCTGGTGGCA
GATGGCAAGTTCGGCACACAGGAGCGGGTGAACAACAGCAACAAGAAGGAGTGGAATGGG
ATGATGGGCGAGCTGCTCAGCGGGCAGGCAGACATGATCGTGGCGCCGCTAACCATAAAC
AACGAGCGCGCGCAGTACATCGAGTTTTCCAAGCCCTTCAAGTACCAGGGCCTGACTATT
CTGGTCAAGAAGGAGATTCCCCGGAGCACGCTGGACTCGTTCATGCAGCCGTTCCAGAGC
ACACTGTGGCTGCTGGTGGGGCTGTCGGTGCACGTGGTGGCCGTGATGCTGTACCTGCTG
GACCGCTTCAGCCCCTTCGGCCGGTTCAAGGTGAACAGCGAGGAGGAGGAGGAGGACGCA
CTGACCCTGTCCTCGGCCATGTGGTTCTCCTGGGGCGTCCTGCTCAACTCCGGCATCGGG
GAAGGCGCCCCCAGAAGCTTCTCAGCGCGCATCCTGGGCATGGTGTGGGCCGGCTTTGCC
ATGATCATCGTGGCCTCCTACACCGCCAACCTGGCGGCCTTCCTGGTGCTGGACCGGCCG
GAGGAGCGCATCACGGGCATCAACGACCCTCGGCTGAGGAACCCCTCGGACAAGTTTATC
TACGCCACGGTGAAGCAGAGCTCCGTGGATATCTACTTCCGGCGCCAGGTGGAGCTGAGC
ACCATGTACCGGCATATGGAGAAGCACAACTACGAGAGTGCGGCGGAGGCCATCCAGGCC
GTGAGAGACAACAAGCTGCATGCCTTCATCTGGGACTCGGCGGTGCTGGAGTTCGAGGCC
TCGCAGAAGTGCGACCTGGTGACGACTGGAGAGCTGTTTTTCCGCTCGGGCTTCGGCATA
GGCATGCGCAAAGACAGCCCCTGGAAGCAGAACGTCTCCCTGTCCATCCTCAAGTCCCAC
GAGAATGGCTTCATGGAAGACCTGGACAAGACGTGGGTTCGGTATCAGGAATGTGACTCG
CGCAGCAACGCCCCTGCGACCCTTACTTTTGAGAACATGGCCGGGGTCTTCATGCTGGTA
GCTGGGGGCATCGTGGCCGGGATCTTCCTGATTTTCATCGAGATTGCCTACAAGCGGCAC
AAGGATGCTCGCCGGAAGCAGATGCAGCTGGCCTTTGCCGCCGTTAACGTGTGGCGGAAG
AACCTGCAGGATAGAAAGAGTGGTAGAGCAGAGCCTGACCCTAAAAAGAAAGCCACATTT
AGGGCTATCACCTCCACCCTGGCTTCCAGCTTCAAGAGGCGTAGGTCCTCCAAAGACACG
AGCACCGGGGGTGGACGCGGCGCTTTGCAAAACCAAAAAGACACAGTGCTGCCGCGACGC
GCTATTGAGAGGGAGGAGGGCCAGCTGCAGCTGTGTTCCCGTCATAGGGAGAGCTGA

1. Karp SJ, Masu M, Eki T, Ozawa K, Nakanishi S: Molecular cloning and chromosomal localization of the key subunit of the human N-methyl-D-aspartate receptor. J Biol Chem. 1993 Feb 15;268(5):3728-33. [PubMed ]
2. Planells-Cases R, Sun W, Ferrer-Montiel AV, Montal M: Molecular cloning, functional expression, and pharmacological characterization of an N-methyl-D-aspartate receptor subunit from human brain. Proc Natl Acad Sci U S A. 1993 Jun 1;90(11):5057-61. [PubMed ]
3. Foldes RL, Rampersad V, Kamboj RK: Cloning and sequence analysis of cDNAs encoding human hippocampus N-methyl-D-aspartate receptor subunits: evidence for alternative RNA splicing. Gene. 1993 Sep 15;131(2):293-8. [PubMed ]
4. Foldes RL, Rampersad V, Kamboj RK: Cloning and sequence analysis of additional splice variants encoding human N-methyl-D-aspartate receptor (hNR1) subunits. Gene. 1994 Sep 30;147(2):303-4. [PubMed ]
5. Younkin DP, Tang CM, Hardy M, Reddy UR, Shi QY, Pleasure SJ, Lee VM, Pleasure D: Inducible expression of neuronal glutamate receptor channels in the NT2 human cell line. Proc Natl Acad Sci U S A. 1993 Mar 15;90(6):2174-8. [PubMed ]
6. Tingley WG, Roche KW, Thompson AK, Huganir RL: Regulation of NMDA receptor phosphorylation by alternative splicing of the C-terminal domain. Nature. 1993 Jul 1;364(6432):70-3. [PubMed ]

1. N-methyl-D-aspartate receptor subtype NR3B
2. NR3B
3. NMDAR3B

MEFVRALWLGLALALGPGSAGGHPQPCGVLARLGGSVRLGALLPRAPLARARARAALARA
ALAPRLPHNLSLELVVAAPPARDPASLTRGLCQALVPPGVAALLAFPEARPELLQLHFLA
AATETPVLSLLRREARAPLGAPNPFHLQLHWASPLETLLDVLVAVLQAHAWEDVGLALCR
TQDPGGLVALWTSRAGRPPQLVLDLSRRDTGDAGLRARLAPMAAPVGGEAPVPAAVLLGC
DIARARRVLEAVPPGPHWLLGTPLPPKALPTAGLPPGLLALGEVARPPLEAAIHDIVQLV
ARALGSAAQVQPKRALLPAPVNCGDLQPAGPESPGRFLARFLANTSFQGRTGPVWVTGSS
QVHMSRHFKVWSLRRDPRGAPAWATVGSWRDGQLDLEPGGASARPPPPQGAQVWPKLRVV
TLLEHPFVFARDPDEDGQCPAGQLCLDPGTNDSATLDALFAALANGSAPRALRKCCYGYC
IDLLERLAEDTPFDFELYLVGDGKYGALRDGRWTGLVGDLLAGRAHMAVTSFSINSARSQ
VVDFTSPFFSTSLGIMVRARDTASPIGAFMWPLHWSTWLGVFAALHLTALFLTVYEWRSP
YGLTPRGRNRSTVFSYSSALNLCYAILFRRTVSSKTPKCPTGRLLMNLWAIFCLLVLSSY
TANLAAVMVGDKTFEELSGIHDPKLHHPAQGFRFGTVWESSAEAYIKKSFPDMHAHMRRH
SAPTTPRGVAMLTSDPPKLNAFIMDKSLLDYEVSIDADCKLLTVGKPFAIEGYGIGLPQN
SPLTSNLSEFISRYKSSGFIDLLHDKWYKMVPCGKRVFAVTETLQMSIYHFAGLFVLLCL
GLGSALLSSLGEHAFFRLALPRIRKGSRLQYWLHTSQKIHRALNTEPPEGSKEETAEAEP
SGPEVEQQQQQQDQPTAPEGWKRARRAVDKERRVRFLLEPAVVVAPEADAEAEAAPREGP
VWLCSYGRPPAARPTGAPQPGELQELERRIEVARERLRQALVRRGQLLAQLGDSARHRPR
RLLQARAAPAEAPPHSGRPGSQE

• Lig_chan (PF00060 )

• 1-22

• 565-585 649-669 831-851

1. Andersson O, Stenqvist A, Attersand A, von Euler G: Nucleotide sequence, genomic organization, and chromosomal localization of genes encoding the human NMDA receptor subunits NR3A and NR3B. Genomics. 2001 Dec;78(3):178-84. [PubMed ]
2. Nishi M, Hinds H, Lu HP, Kawata M, Hayashi Y: Motoneuron-specific expression of NR3B, a novel NMDA-type glutamate receptor subunit that works in a dominant-negative manner. J Neurosci. 2001 Dec 1;21(23):RC185. [PubMed ]

1. N-methyl D- aspartate receptor subtype 2B
2. NR2B
3. NMDAR2B
4. N-methyl-D-aspartate receptor subunit 3
5. NR3
6. hNR3

MKPRAECCSPKFWLVLAVLAVSGSRARSQKSPPSIGIAVILVGTSDEVAIKDAHEKDDFH
HLSVVPRVELVAMNETDPKSIITRICDLMSDRKIQGVVFADDTDQEAIAQILDFISAQTL
TPILGIHGGSSMIMADKDESSMFFQFGPSIEQQASVMLNIMEEYDWYIFSIVTTYFPGYQ
DFVNKIRSTIENSFVGWELEEVLLLDMSLDDGDSKIQNQLKKLQSPIILLYCTKEEATYI
FEVANSVGLTGYGYTWIVPSLVAGDTDTVPAEFPTGLISVSYDEWDYGLPARVRDGIAII
TTAASDMLSEHSFIPEPKSSCYNTHEKRIYQSNMLNRYLINVTFEGRNLSFSEDGYQMHP
KLVIILLNKERKWERVGKWKDKSLQMKYYVWPRMCPETEEQEDDHLSIVTLEEAPFVIVE
SVDPLSGTCMRNTVPCQKRIVTENKTDEEPGYIKKCCKGFCIDILKKISKSVKFTYDLYL
VTNGKHGKKINGTWNGMIGEVVMKRAYMAVGSLTINEERSEVVDFSVPFIETGISVMVSR
SNGTVSPSAFLEPFSADVWVMMFVMLLIVSAVAVFVFEYFSPVGYNRCLADGREPGGPSF
TIGKAIWLLWGLVFNNSVPVQNPKGTTSKIMVSVWAFFAVIFLASYTANLAAFMIQEEYV
DQVSGLSDKKFQRPNDFSPPFRFGTVPNGSTERNIRNNYAEMHAYMGKFNQRGVDDALLS
LKTGKLDAFIYDAAVLNYMAGRDEGCKLVTIGSGKVFASTGYGIAIQKDSGWKRQVDLAI
LQLFGDGEMEELEALWLTGICHNEKNEVMSSQLDIDNMAGVFYMLGAAMALSLITFICEH
LFYWQFRHCFMGVCSGKPGMVFSISRGIYSCIHGVAIEERQSVMNSPTATMNNTHSNILR
LLRTAKNMANLSGVNGSPQSALDFIRRESSVYDISEHRRSFTHSDCKSYNNPPCEENLFS
DYISEVERTFGNLQLKDSNVYQDHYHHHHRPHSIGSASSIDGLYDCDNPPFTTQSRSISK
KPLDIGLPSSKHSQLSDLYGKFSFKSDRYSGHDDLIRSDVSDISTHTVTYGNIEGNAAKR
RKQQYKDSLKKRPASAKSRREFDEIELAYRRRPPRSPDHKRYFRDKEGLRDFYLDQFRTK
ENSPHWEHVDLTDIYKERSDDFKRDSVSGGGPCTNRSHIKHGTGDKHGVVSGVPAPWEKN
LTNVEWEDRSGGNFCRSCPSKLHNYSTTVTGQNSGRQACIRCEACKKAGNLYDISEDNSL
QELDQPAAPVAVTSNASTTKYPQSPTNSKAQKKNRNKLRRQHSYDTFVDLQKEEAALAPR
SVSLKDKGRFMDGSPYAHMFEMSAGESTFANNKSSVPTAGHHHHNNPGGGYMLSKSLYPD
RVTQNPFIPTFGDDQCLLHGSKSYFFRQPTVAGASKARPDFRALVTNKPVVSALHGAVPA
RFQKDICIGNQSNPCVPNNKNPRAFNGSSNGHVYEKLSSIESDV

• Lig_chan (PF00060 )

• 1-26

• 558-578 635-655 818-838

ATGAAGCCCAGAGCGGAGTGCTGTTCTCCCAAGTTCTGGTTGGTGTTGGCCGTCCTGGCC
GTGTCAGGCAGCAGAGCTCGTTCTCAGAAGAGCCCCCCCAGCATTGGCATTGCTGTCATC
CTCGTGGGCACTTCCGACGAGGTGGCCATCAAGGATGCCCACGAGAAAGATGATTTCCAC
CATCTCTCCGTGGTACCCCGGGTGGAACTGGTAGCCATGAATGAGACCGACCCAAAGAGC
ATCATCACCCGCATCTGTGATCTCATGTCTGACCGGAAGATCCAGGGGGTGGTGTTTGCT
GATGACACAGACCAGGAAGCCATCGCCCAGATCCTCGATTTCATTTCAGCACAGACTCTC
ACCCCGATCCTGGGCATCCACGGGGGCTCCTCTATGATAATGGCAGATAAGGATGAATCC
TCCATGTTCTTCCAGTTTGGCCCATCAATTGAACAGCAAGCTTCCGTAATGCTCAACATC
ATGGAAGAATATGACTGGTACATCTTTTCTATCGTCACCACCTATTTCCCTGGCTACCAG
GACTTTGTAAACAAGATCCGCAGCACCATTGAGAATAGCTTTGTGGGCTGGGAGCTAGAG
GAGGTCCTCCTACTGGACATGTCCCTGGACGATGGAGATTCTAAGATCCAGAATCAGCTC
AAGAAACTTCAAAGCCCCATCATTCTTCTTTACTGTACCAAGGAAGAAGCCACCTACATC
TTTGAAGTGGCCAACTCAGTAGGGCTGACTGGCTATGGCTACACGTGGATCGTGCCCAGT
CTGGTGGCAGGGGATACAGACACAGTGCCTGCGGAGTTCCCCACTGGGCTCATCTCTGTA
TCATATGATGAATGGGACTATGGCCTCCCCGCCAGAGTGAGAGATGGAATTGCCATAATC
ACCACTGCTGCTTCTGACATGCTGTCTGAGCACAGCTTCATCCCTGAGCCCAAAAGCAGT
TGTTACAACACCCACGAGAAGAGAATCTACCAGTCCAATATGCTAAATAGGTATCTGATC
AATGTCACTTTTGAGGGGAGGAATTTGTCCTTCAGTGAAGATGGCTACCAGATGCACCCG
AAACTGGTGATAATTCTTCTGAACAAGGAGAGGAAGTGGGAAAGGGTGGGGAAGTGGAAA
GACAAGTCCCTGCAGATGAAGTACTATGTGTGGCCCCGAATGTGTCCAGAGACTGAAGAG
CAGGAGGATGACCATCTGAGCATTGTGACCCTGGAGGAGGCACCATTTGTCATTGTGGAA
AGTGTGGACCCTCTGAGTGGAACCTGCATGAGGAACACAGTCCCCTGCCAAAAACGCATA
GTCACTGAGAATAAAACAGACGAGGAGCCGGGTTACATCAAAAAATGCTGCAAGGGGTTC
TGTATTGACATCCTTAAGAAAATTTCTAAATCTGTGAAGTTCACCTATGACCTTTACCTG
GTTACCAATGGCAAGCATGGGAAGAAAATCAATGGAACCTGGAATGGTATGATTGGAGAG
GTGGTCATGAAGAGGGCCTACATGGCAGTGGGCTCACTCACCATCAATGAGGAACGATCG
GAGGTGGTCGACTTCTCTGTGCCCTTCATAGAGACAGGCATCAGTGTCATGGTGTCACGC
AGCAATGGGACTGTCTCACCTTCTGCCTTCTTAGAGCCATTCAGCGCTGACGTATGGGTG
ATGATGTTTGTGATGCTGCTCATCGTCTCAGCCGTGGCTGTCTTTGTCTTTGAGTACTTC
AGCCCTGTGGGTTATAACAGGTGCCTCGCTGATGGCAGAGAGCCTGGTGGACCCTCTTTC
ACCATCGGCAAAGCTATTTGGTTGCTCTGGGGTCTGGTGTTTAACAACTCCGTACCTGTG
CAGAACCCAAAGGGGACCACCTCCAAGATCATGGTGTCAGTGTGGGCCTTCTTTGCTGTC
ATCTTCCTGGCCAGCTACACTGCCAACTTAGCTGCCTTCATGATCCAAGAGGAATATGTG
GACCAGGTTTCTGGCCTGAGCGACAAAAAGTTCCAGAGACCTAATGACTTCTCACCCCCT
TTCCGCTTTGGGACCGTGCCCAACGGCAGCACAGAGAGAAATATTCGCAATAACTATGCA
GAAATGCATGCCTACATGGGAAAGTTCAACCAGAGGGGTGTAGATGATGCATTGCTCTCC
CTGAAAACAGGGAAACTGGATGCCTTCATCTATGATGCAGCAGTGCTGAACTATATGGCA
GGCAGAGATGAAGGCTGCAAGCTGGTGACCATTGGCAGTGGGAAGGTCTTTGCTTCCACT
GGCTATGGCATTGCCATCCAAAAAGATTCTGGGTGGAAGCGCCAGGTGGACCTTGCTATC
CTGCAGCTCTTTGGAGATGGGGAGATGGAAGAACTGGAAGCTCTCTGGCTCACTGGCATT
TGTCACAATGAGAAGAATGAGGTCATGAGCAGCCAGCTGGACATTGACAACATGGCAGGG
GTCTTCTACATGTTGGGGGCGGCCATGGCTCTCAGCCTCATCACCTTCATCTGCGAACAC
CTTTTCTATTGGCAGTTCCGACATTGCTTTATGGGTGTCTGTTCTGGCAAGCCTGGCATG
GTCTTCTCCATCAGCAGAGGTATCTACAGCTGCATCCATGGGGTGGCGATCGAGGAGCGC
CAGTCTGTAATGAACTCCCCCACCGCAACCATGAACAACACACACTCCAACATCCTGCGC
CTGCTGCGCACGGCCAAGAACATGGCTAACCTGTCTGGTGTGAATGGCTCACCGCAGAGC
GCCCTGGACTTCATCCGACGGGAGTCATCCGTCTATGACATCTCAGAGCACCGCCGCAGC
TTCACGCATTCTGACTGCAAATCCTACAACAACCCGCCCTGTGAGGAGAACCTCTTCAGT
GACTACATCAGTGAGGTAGAGAGAACGTTCGGGAACCTGCAGCTGAAGGACAGCAACGTG
TACCAAGATCACTACCACCATCACCACCGGCCCCATAGTATTGGCAGTGCCAGCTCCATC
GATGGGCTCTACGACTGTGACAACCCACCCTTCACCACCCAGTCCAGGTCCATCAGCAAG
AAGCCCCTGGACATCGGCCTCCCCTCCTCCAAGCACAGCCAGCTCAGTGACCTGTACGGC
AAATTCTCCTTCAAGAGCGACCGCTACAGTGGCCACGACGACTTGATCCGCTCCGATGTC
TCTGACATCTCAACCCACACCGTCACCTATGGGAACATCGAGGGCAATGCCGCCAAGAGG
CGTAAGCAGCAATATAAGGACAGCCTGAAGAAGCGGCCTGCCTCGGCCAAGTCCCGCAGG
GAGTTTGACGAGATCGAGCTGGCCTACCGTCGCCGACCGCCCCGCTCCCCTGACCACAAG
CGCTACTTCAGGGACAAGGAAGGGCTACGGGACTTCTACCTGGACCAGTTCCGAACAAAG
GAGAACTCACCCCACTGGGAGCACGTAGACCTGACCGACATCTACAAGGAGCGGAGTGAT
GACTTTAAGCGCGACTCCATCAGCGGAGGAGGGCCCTGTACCAACAGGTCTCACATCAAG
CACGGGACGGGCGACAAACACGGCGTGGTCAGCGGGGTACCTGCACCTTGGGAGAAGAAC
CTGACCAACGTGGAGTGGGAGGACCGGTCCGGGGGCAACTTCTGCCGCAGCTGTCCCTCC
AAGCTGCACAACTACTCCACGACGGTGACGGGTCAGAACTCGGGCAGGCAGGCGTGCATC
CGGTGTGAGGCTTGCAAGAAAGCAGGCAACCTGTATGACATCAGTGAGGACAACTCCCTG
CAGGAACTGGACCAGCCGGCTGCCCCAGTGGCGGTGACGTCAAACGCCTCCACCACTAAG
TACCCTCAGAGCCCGACTAATTCCAAGGCCCAGAAGAAGAACCGGAACAAACTGCGCCGG
CAGCACTCCTACGACACCTTCGTGGACCTGCAGAAGGAAGAAGCCGCCCTGGCCCCGCGC
AGCGTAAGCCTGAAAGACAAGGGCCGATTCATGGATGGGAGCCCCTACGCCCACATGTTT
GAGATGTCAGCTGGCGAGAGCACCTTTGCCAACAACAAGTCCTCAGTGCCCACTGCCGGA
CATCACCACCACAACAACCCCGGCGGCGGGTACATGCTCAGCAAGTCGCTCTACCCTGAC
CGGGTCACGCAAAACCCTTTCATCCCCACTTTTGGGGACGACCAGTGCTTGCTCCATGGC
AGCAAATCCTACTTCTTCAGGCAGCCCACGGTGGCGGGGGCGTCGAAAGCCAGGCCGGAC
TTCCGGGCCCTTGTCACCAACAAGCCGGTGGTCTCGGCCCTTCATGGGGCCGTGCCAGCC
CGTTTCCAGAAGGACATCTGTATAGGGAACCAGTCCAACCCCTGTGTGCCTAACAACAAA
AACCCCAGGGCTTTCAATGGCTCCAGCAATGGGCATGTTTATGAGAAACTTTCTAGTATT
GAGTCTGATGTCTGA

1. Adams SL, Foldes RL, Kamboj RK: Human N-methyl-D-aspartate receptor modulatory subunit hNR3: cloning and sequencing of the cDNA and primary structure of the protein. Biochim Biophys Acta. 1995 Jan 2;1260(1):105-8. [PubMed ]
2. Hess SD, Daggett LP, Crona J, Deal C, Lu CC, Urrutia A, Chavez-Noriega L, Ellis SB, Johnson EC, Velicelebi G: Cloning and functional characterization of human heteromeric N-methyl-D-aspartate receptors. J Pharmacol Exp Ther. 1996 Aug;278(2):808-16. [PubMed ]
3. Mandich P, Schito AM, Bellone E, Antonacci R, Finelli P, Rocchi M, Ajmar F: Mapping of the human NMDAR2B receptor subunit gene (GRIN2B) to chromosome 12p12. Genomics. 1994 Jul 1;22(1):216-8. [PubMed ]
4. Schito AM, Pizzuti A, Di Maria E, Schenone A, Ratti A, Defferrari R, Bellone E, Mancardi GL, Ajmar F, Mandich P: mRNA distribution in adult human brain of GRIN2B, a N-methyl-D-aspartate (NMDA) receptor subunit. Neurosci Lett. 1997 Dec 12;239(1):49-53. [PubMed ]

1. Gamma-glutamyl carboxylase
2. Vitamin K gamma glutamyl carboxylase

MAVSAGSARTSPSSDKVQKDKAELISGPRQDSRIGKLLGFEWTDLSSWRRLVTLLNRPTD
PASLAVFRFLFGFLMVLDIPQERGLSSLDRKYLDGLDVCRFPLLDALRPLPLDWMYLVYT
IMFLGALGMMLGLCYRISCVLFLLPYWYVFLLDKTSWNNHSYLYGLLAFQLTFMDANHYW
SVDGLLNAHRRNAHVPLWNYAVLRGQIFIVYFIAGVKKLDADWVEGYSMEYLSRHWLFSP
FKLLLSEELTSLLVVHWGGLLLDLSAGFLLFFDVSRSIGLFFVSYFHCMNSQLFSIGMFS
YVMLASSPLFCSPEWPRKLVSYCPRRLQQLLPLKAAPQPSVSCVYKRSRGKSGQKPGLRH
QLGAAFTLLYLLEQLFLPYSHFLTQGYNNWTNGLYGYSWDMMVHSRSHQHVKITYRDGRT
GELGYLNPGVFTQSRRWKDHADMLKQYATCLSRLLPKYNVTEPQIYFDIWVSINDRFQQR
IFDPRVDIVQAAWSPFQRTSWVQPLLMDLSPWRAKLQEIKSSLDNHTEVVFIADFPGLHL
ENFVSEDLGNTSIQLLQGEVTVELVAEQKNQTLREGEKMQLPAGEYHKVYTTSPSPSCYM
YVYVNTTELALEQDLAYLQELKEKVENGSETGPLPPELQPLLEGEVKGGPEPTPLVQTFL
RRQQRLQEIERRRNTPFHERFFRFLLRKLYVFRRSFLMTCISLRNLILGRPSLEQLAQEV
TYANLRPFEAVGELNPSNTDSSHSNPPESNPDPVHSEF

• VKG_Carbox (PF05090 )

• None

• 61-81 114-134 137-157 293-313 362-382